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  • Base Sequence  (120)
  • American Association for the Advancement of Science (AAAS)  (120)
  • American Association of Petroleum Geologists (AAPG)
  • Cambridge University Press
  • 1990-1994  (120)
  • 1975-1979
  • 1991  (120)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (120)
  • American Association of Petroleum Geologists (AAPG)
  • Cambridge University Press
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  • 1990-1994  (120)
  • 1975-1979
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  • 1
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    The combination of symbolic and numerical computation for three-dimensional modeling of RNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-13
    Description: Three-dimensional (3-D) structural models of RNA are essential for understanding of the cellular roles played by RNA. Such models have been obtained by a technique based on a constraint satisfaction algorithm that allows for the facile incorporation of secondary and other structural information. The program generates 3-D structures of RNA with atomic-level resolution that can be refined by numerical techniques such as energy minimization. The precision of this technique was evaluated by comparing predicted transfer RNA loop and RNA pseudoknot structures with known or consensus structures. The root-mean-square deviation (2.0 to 3.0 angstroms before minimization) between predicted and control structures reveal this system to be an effective method in modeling RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Major, F -- Turcotte, M -- Gautheret, D -- Lapalme, G -- Fillion, E -- Cedergren, R -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1255-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement d'Informatique et de Recherche Operationnelle, Universite de Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716375" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Anticodon/chemistry ; Base Sequence ; *Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/*chemistry ; RNA, Transfer/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 2
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    A multisubunit ribozyme that is a catalyst of and template for complementary strand RNA synthesis (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-29
    Description: Derivatives of the sunY self-splicing intron efficiently catalyzed the synthesis of complementary strand RNA by template-directed assembly of oligonucleotides. These ribozymes were separated into three short RNA fragments that formed active catalytic complexes. One of the multisubunit sunY derivatives catalyzed the synthesis of a strand of RNA complementary to one of its own subunits. These results suggest that prebiotically synthesized oligonucleotides might have been able to assemble into a complex capable of self-replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doudna, J A -- Couture, S -- Szostak, J W -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1605-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1707185" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; *Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/metabolism ; RNA/*biosynthesis/genetics ; RNA Splicing ; RNA, Catalytic/*metabolism ; Templates, Genetic ; Tetrahymena/*genetics
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  • 3
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    Group I intron self-splicing with adenosine: evidence for a single nucleoside-binding site (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-19
    Description: For self-splicing of Tetrahymena ribosomal RNA precursor, guanosine binding is required for 5' splice-site cleavage and exon ligation. Whether these two reactions use the same or different guanosine-binding sites has been debated. A double mutation in a previously identified guanosine-binding site within the intron resulted in preference for adenosine (or adenosine triphosphate) as the substrate for cleavage at the 5' splice site. However, splicing was blocked in the exon ligation step. Blockage was reversed by a change from guanine to adenine at the 3' splice site. These results indicate that a single determinant specifies nucleoside binding for both steps of splicing. Furthermore, it suggests that RNA could form an active site specific for adenosine triphosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Been, M D -- Perrotta, A T -- GM-40689/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):434-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017681" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*metabolism ; Adenosine Triphosphate/pharmacology ; Animals ; Base Sequence ; Binding Sites ; Exons ; Guanosine/metabolism ; *Introns ; Magnesium/pharmacology ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis ; RNA Precursors/chemistry/genetics ; *RNA Splicing ; RNA, Catalytic/metabolism ; Tetrahymena/genetics
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  • 4
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    Identification of the DNA binding site for NGFI-B by genetic selection in yeast (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: An in vivo selection system for isolating targets of DNA binding proteins in yeast was developed and used to identify the DNA binding site for the NGFI-B protein, a member of the steroid-thyroid hormone receptor superfamily. The feasibility of the technique was verified by selecting DNA fragments that contained binding sites for GCN4, a well-characterized yeast transcriptional activator. The DNA binding domain of NGFI-B, expressed as part of a LexA-NGFI-B-GAL4 chimeric activator, was then used to isolate a rat genomic DNA fragment that contained an NGFI-B binding site. The NGFI-B response element (NBRE) is similar to but functionally distinct from elements recognized by the estrogen and thyroid hormone receptors and the hormone receptor-like proteins COUP-TF, CF1, and H-2RIIBP. Cotransfection experiments in mammalian cells demonstrated that NGFI-B can activate transcription from the NBRE with or without its putative ligand binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Fahrner, T J -- Johnston, M -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1296-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/*metabolism ; DNA-Binding Proteins/genetics/*metabolism/pharmacology ; Fungal Proteins/metabolism ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Plasmids ; *Protein Kinases ; Rats ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Repressor Proteins ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; *Serine Endopeptidases ; Transcription Factors/genetics/*metabolism/pharmacology ; Transcription, Genetic ; Transfection
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  • 5
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    Isolation of an active human transposable element (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-30
    Description: Two de novo insertions of truncated L1 elements into the factor VIII gene on the X chromosome have been identified that produced hemophilia A. A full-length L1 element that is the likely progenitor of one of these insertions was isolated by its sequence identity to the factor VIII insertion. This L1 element contains two open-reading frames and is one of at least four alleles of a locus on chromosome 22 that has been occupied by an L1 element for at least 6 million years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dombroski, B A -- Mathias, S L -- Nanthakumar, E -- Scott, A F -- Kazazian, H H Jr -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1662412" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosomes, Human, Pair 22 ; *DNA Transposable Elements ; Factor VIII/*genetics ; Genome, Human ; Hemophilia A/*genetics ; Humans ; Molecular Sequence Data ; Open Reading Frames ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; X Chromosome
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  • 6
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    Repression of HIV-1 transcription by a cellular protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-22
    Description: A cellular DNA binding protein, LBP-1, sequentially interacts in a concentration-dependent manner with two sites that surround the transcriptional initiation site of the human immunodeficiency virus type 1 (HIV-1) promoter. Although sequences in the downstream site (site I) were found to enhance transcription, purified LBP-1 specifically repressed transcription in vitro by binding to the upstream site (site II), which overlaps the TATA element. The binding of human TATA binding factor (TFIID) to the promoter before LBP-1 blocked repression, suggesting that repression resulted from an inhibition of TFIID binding to the TATA element. Furthermore, mutations that eliminated binding to site II both prevented repression in vitro and increased HIV-1 transcription in stably transformed cells. These findings suggest that a cellular factor regulates HIV-1 transcription in a manner that is characteristic of bacterial repressors and that this factor could be important in HIV-1 latency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kato, H -- Horikoshi, M -- Roeder, R G -- AI27397/AI/NIAID NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1476-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006421" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/genetics ; *Gene Expression Regulation, Viral ; HIV-1/*genetics ; Molecular Sequence Data ; Promoter Regions, Genetic ; Repressor Proteins/*genetics ; Transcription Factor TFIID ; Transcription Factors/metabolism ; Transcription, Genetic
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  • 7
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    Identification of p53 gene mutations in bladder cancers and urine samples (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: Although bladder cancers are very common, little is known about their molecular pathogenesis. In this study, invasive bladder cancers were evaluated for the presence of gene mutations in the p53 suppressor gene. Of 18 tumors evaluated, 11 (61 percent) were found to have genetic alterations of p53. The alterations included ten point mutations resulting in single amino acid substitutions, and one 24-base pair deletion. In all but one case, the mutations were associated with chromosome 17p allelic deletions, leaving the cells with only mutant forms of the p53 gene products. Through the use of the polymerase chain reaction and oligomer-specific hybridization, p53 mutations were identified in 1 to 7 percent of the cells within the urine sediment of each of three patients tested. The p53 mutations are the first genetic alterations demonstrated to occur in a high proportion of primary invasive bladder cancers. Detection of such mutations ex vivo has clinical implications for monitoring individuals whose tumor cells are shed extracorporeally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidransky, D -- Von Eschenbach, A -- Tsai, Y C -- Jones, P -- Summerhayes, I -- Marshall, F -- Paul, M -- Green, P -- Hamilton, S R -- Frost, P -- CA09071/CA/NCI NIH HHS/ -- CA43460/CA/NCI NIH HHS/ -- CA49758/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):706-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024123" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Deletion ; Chromosomes, Human, Pair 17 ; *Genes, p53 ; Humans ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Urinary Bladder Neoplasms/*genetics/urine ; Urine/cytology
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  • 8
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    Function of the homeodomain protein GHF1 in pituitary cell proliferation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: Mutations that cause pituitary dwarfism in the mouse reside in the gene encoding the transcription factor growth hormone factor 1 (GHF1 or pit1). These dwarf mice (dw and dwJ) are deficient in growth hormone (GH) and prolactin (PRL) synthesis and exhibit pituitary hypoplasia, suggesting a stem cell defect. With antisense oligonucleotide technology, a cell culture model of this genetic defect was developed. Specific inhibition of GHF1 synthesis by complementary oligonucleotides led to a marked decrease in GH and PRL expression and to a marked decrease in proliferation of somatotrophic cell lines. These results provide direct evidence that the homeodomain protein GHF1 is required not only for the establishment and maintenance of the differentiated phenotype but for cell proliferation as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castrillo, J L -- Theill, L E -- Karin, M -- DK38527/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antisense Elements (Genetics) ; Base Sequence ; *Cell Division ; Cells, Cultured ; DNA/biosynthesis ; DNA-Binding Proteins/*physiology ; Dwarfism/genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Growth Hormone/genetics ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Pituitary Gland/*cytology/physiology ; Prolactin/genetics ; Transcription Factor Pit-1 ; Transcription Factors/*physiology
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  • 9
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    Cloning and expression of a cocaine-sensitive rat dopamine transporter (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The action of dopamine and other monoamine neurotransmitters at synapses is terminated predominantly by high-affinity reuptake into presynaptic terminals by specific sodium-dependent neurotransmitter transport proteins. A complementary DNA encoding a rat dopamine transporter has been isolated that exhibits high sequence similarity with the previously cloned norepinephrine and gamma-aminobutyric acid transporters. Transient expression of the complementary DNA in HeLa cells confirms the cocaine sensitivity of this transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilty, J E -- Lorang, D -- Amara, S G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cloning, Molecular ; Cocaine/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Gene Expression ; HeLa Cells ; Humans ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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  • 10
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    A genetic model for interaction of the homeodomain recognition helix with DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-25
    Description: The Bicoid homeodomain protein controls anterior development in the Drosophila embryo by binding to DNA and regulating gene expression. With the use of genetic assays in yeast, the interaction between the Bicoid homeodomain and a series of mutated DNA sites was studied. These experiments defined important features of homeodomain binding sites, identified specific amino acid-base pair contacts, and suggested a model for interaction of the recognition alpha-helices of Bicoid and Antennapedia-class homeodomain proteins with DNA. The model is in general agreement with results of crystallographic and magnetic resonance studies, but differs in important details. It is likely that genetic studies of protein-DNA interaction will continue to complement conventional structural approaches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanes, S D -- Brent, R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):426-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1671176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/*metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Drosophila ; Gene Expression Regulation ; Genes, Homeobox/*genetics ; *Homeodomain Proteins ; Insect Hormones/*genetics/metabolism ; *Models, Genetic ; Molecular Sequence Data ; *Trans-Activators ; Transcription, Genetic
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  • 11
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    Visualizing the higher order folding of a catalytic RNA molecule (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-25
    Description: The higher order folding process of the catalytic RNA derived from the self-splicing intron of Tetrahymena thermophila was monitored with the use of Fe(II)-EDTA-induced free radical chemistry. The overall tertiary structure of the RNA molecule forms cooperatively with the uptake of at least three magnesium ions. Local folding transitions display different metal ion dependencies, suggesting that the RNA tertiary structure assembles through a specific folding intermediate before the catalytic core is formed. Enzymatic activity, assayed with an RNA substrate that is complementary to the catalytic RNA active site, coincides with the cooperative structural transition. The higher order RNA foldings produced by Mg(II), Ca(II), and Sr(II) are similar; however, only the Mg(II)-stabilized RNA is catalytically active. Thus, these results directly demonstrate that divalent metal ions participate in general folding of the ribozyme tertiary structure, and further indicate a more specific involvement of Mg(II) in catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celander, D W -- Cech, T R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):401-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1989074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Calcium/metabolism ; Densitometry ; Kinetics ; Magnesium/metabolism ; Magnesium Chloride/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/drug effects/metabolism ; Strontium/metabolism ; Tetrahymena
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  • 12
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    Resistance to ddI and sensitivity to AZT induced by a mutation in HIV-1 reverse transcriptase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-27
    Description: Serial human immunodeficiency virus type-1 (HIV-1) isolates were obtained from five individuals with acquired immunodeficiency syndrome (AIDS) who changed therapy to 2',3'-dideoxyinosine (ddI) after at least 12 months of treatment with 3'-azido-3'-deoxythymidine (zidovudine, AZT). The in vitro sensitivity to ddI decreased during the 12 months following ddI initiation, whereas AZT sensitivity increased. Analysis of the reverse transcriptase coding region revealed a mutation associated with reduced sensitivity to ddI. When this mutation was present in the same genome as a mutation known to confer AZT resistance, the isolates showed increased sensitivity to AZT. Analysis of HIV-1 variants confirmed that the ddI resistance mutation alone conferred ddI and 2',3'-dideoxycytidine resistance, and suppressed the effect of the AZT resistance mutation. The use of combination therapy for HIV-1 disease may prevent drug-resistant isolates from emerging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St Clair, M H -- Martin, J L -- Tudor-Williams, G -- Bach, M C -- Vavro, C L -- King, D M -- Kellam, P -- Kemp, S D -- Larder, B A -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1557-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Virology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716788" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*drug therapy/microbiology ; Base Sequence ; DNA, Viral/*genetics ; Didanosine/*pharmacology/*therapeutic use ; Drug Resistance, Microbial ; Genotype ; HIV-1/*drug effects/enzymology/isolation & purification ; Humans ; Molecular Sequence Data ; *Mutation ; Oligodeoxyribonucleotides ; RNA-Directed DNA Polymerase/*genetics/metabolism ; Zidovudine/pharmacology/*therapeutic use
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  • 13
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    Exchange of conduction pathways between two related K+ channels (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-22
    Description: The structure of the ion conduction pathway or pore of voltage-gated ion channels is unknown, although the linker between the membrane spanning segments S5 and S6 has been suggested to form part of the pore in potassium channels. To test whether this region controls potassium channel conduction, a 21-amino acid segment of the S5-S6 linker was transplanted from the voltage-activated potassium channel NGK2 to another potassium channel DRK1, which has very different pore properties. In the resulting chimeric channel, the single channel conductance and blockade by external and internal tetraethylammonium (TEA) ion were characteristic of the donor NGK2 channel. Thus, this 21-amino acid segment controls the essential biophysical properties of the pore and may form the conduction pathway of these potassium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartmann, H A -- Kirsch, G E -- Drewe, J A -- Taglialatela, M -- Joho, R H -- Brown, A M -- NS08805/NS/NINDS NIH HHS/ -- NS23877/NS/NINDS NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):942-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/physiology ; Chimera ; Cloning, Molecular ; Female ; Ion Channel Gating ; Membrane Potentials ; Molecular Sequence Data ; Oligonucleotide Probes ; Oocytes/physiology ; Polymerase Chain Reaction ; Potassium Channels/drug effects/genetics/*physiology ; Rats ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Xenopus
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  • 14
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    Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-14
    Description: In the interleukin-2 (IL-2) system, intracellular signal transduction is triggered by the beta chain of the IL-2 receptor (IL-2R beta); however, the responsible signaling mechanism remains unidentified. Evidence for the formation of a stable complex of IL-2R beta and the lymphocyte-specific protein tyrosine kinase p56lck is presented. Specific association sites were identified in the tyrosine kinase catalytic domain of p56lck and in the cytoplasmic domain of IL-2R beta. As a result of interaction, IL-2R beta became phosphorylated in vitro by p56lck. Treatment of T lymphocytes with IL-2 promotes p56lck kinase activity. These data suggest the participation of p56lck as a critical signaling molecule downstream of IL-2R via a novel interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatakeyama, M -- Kono, T -- Kobayashi, N -- Kawahara, A -- Levin, S D -- Perlmutter, R M -- Taniguchi, T -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1523-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047859" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Antigens, CD/immunology ; Base Sequence ; Binding Sites ; Cell Division/drug effects ; Cell Line ; Humans ; Interleukin-2/pharmacology ; Killer Cells, Natural/cytology/drug effects/immunology ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Lymphocytes/drug effects/*immunology ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Protein-Tyrosine Kinases/genetics/isolation & purification/*metabolism ; Receptors, Interleukin-2/genetics/isolation & purification/*physiology ; *Signal Transduction ; Transfection
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  • 15
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    Deregulation of a homeobox gene, HOX11, by the t(10;14) in T cell leukemia (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-05
    Description: Molecular cloning of the t(10;14)(q24;q11) recurrent breakpoint of T cell acute lymphoblastic leukemia has demonstrated a transcript for the candidate gene TCL3. Characterization of this gene from chromosome segment 10q24 revealed it to be a new homeobox, HOX11. The HOX11 homeodomain is most similar to that of the murine gene Hlx and possesses a markedly glycine-rich variable region and an acidic carboxyl terminus. HOX11, while expressed in liver, was not detected in normal thymus or T cells. This lineage-restricted homeobox gene is deregulated upon translocation into the T cell receptor locus where it may act as an oncogene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatano, M -- Roberts, C W -- Minden, M -- Crist, W M -- Korsmeyer, S J -- 1 PO1 CA49712/CA/NCI NIH HHS/ -- CA 21765/CA/NCI NIH HHS/ -- CA 30969/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1676542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Chromosomes, Human, Pair 10 ; Chromosomes, Human, Pair 14 ; Cloning, Molecular ; *Gene Expression Regulation, Neoplastic ; *Genes, Homeobox ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; *Translocation, Genetic
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  • 16
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    Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The most frequently occurring RNA hairpins in 16S and 23S ribosomal RNA contain a tetranucleotide loop that has a GNRA consensus sequence. The solution structures of the GCAA and GAAA hairpins have been determined by nuclear magnetic resonance spectroscopy. Both loops contain an unusual G-A base pair between the first and last residue in the loop, a hydrogen bond between a G base and a phosphate, extensive base stacking, and a hydrogen bond between a sugar 2'-end OH and a base. These interactions explain the high stability of these hairpins and the sequence requirements for the variant and invariant nucleotides in the GNRA tetranucleotide loop family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heus, H A -- Pardi, A -- AI 27026/AI/NIAID NIH HHS/ -- AI 30726/AI/NIAID NIH HHS/ -- RR03283/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):191-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1712983" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Graphics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry ; RNA/chemistry/*ultrastructure ; Structure-Activity Relationship ; Thermodynamics
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  • 17
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    Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: Dioxin (2,3,7,8-tetrachlorodibenzo-p-dioxin, TCDD), a widespread environmental contaminant, may elicit its effects by altering gene expression in susceptible cells. Five TCDD-responsive complementary DNA clones were isolated from a human keratinocyte cell line. One of these clones encodes plasminogen activator inhibitor-2, a factor that influences growth and differentiation by regulating proteolysis of the extracellular matrix. Another encodes the cytokine interleukin-1 beta. Thus, TCDD alters the expression of growth regulatory genes and has effects similar to those of other tumor-promoting agents that affect both inflammation and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sutter, T R -- Guzman, K -- Dold, K M -- Greenlee, W F -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Industry Institute of Toxicology, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925598" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blood Physiological Phenomena ; Blotting, Northern ; Calcium/pharmacology ; Cell Line ; Cloning, Molecular ; Cycloheximide/pharmacology ; Gene Expression Regulation/drug effects ; Humans ; Interleukin-1/*genetics ; *Plasminogen Inactivators ; RNA, Messenger/drug effects ; Tetrachlorodibenzodioxin/*pharmacology ; Transcription, Genetic/drug effects
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  • 18
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    Mapping of DNA instability at the fragile X to a trinucleotide repeat sequence p(CCG)n (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-21
    Description: The sequence of a Pst I restriction fragment was determined that demonstrate instability in fragile X syndrome pedigrees. The region of instability was localized to a trinucleotide repeat p(CCG)n. The sequence flanking this repeat were identical in normal and affected individuals. The breakpoints in two somatic cell hybrids constructed to break at the fragile site also mapped to this repeat sequence. The repeat exhibits instability both when cloned in a nonhomologous host and after amplification by the polymerase chain reaction. These results suggest variation in the trinucleotide repeat copy number as the molecular basis for the instability and possibly the fragile site. This would account for the observed properties of this region in vivo and in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kremer, E J -- Pritchard, M -- Lynch, M -- Yu, S -- Holman, K -- Baker, E -- Warren, S T -- Schlessinger, D -- Sutherland, G R -- Richards, R I -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1711-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cytogenetics and Molecular Genetics, Adelaide Children's Hospital, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1675488" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Fragile X Syndrome/*genetics ; Humans ; Molecular Sequence Data ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping ; X Chromosome/ultrastructure
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  • 19
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    HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: In simple eukaryotes, protein kinases regulate mitotic and meiotic cell cycles, the response to polypeptide pheromones, and the initiation of nuclear DNA synthesis. The protein HRR25 from the budding yeast Saccharomyces cerevisiae was defined by the mutation hrr25-1. This mutation resulted in sensitivity to continuous expression of the HO double-strand endonuclease, to methyl methanesulfonate, and to x-irradiation. Homozygotes of hrr25-1 were unable to sporulate and disruption and deletion of HRR25 interfered with mitotic and meiotic cell division. Sequence analysis revealed two distinctive regions in the protein. The NH2-terminus of HRR25 contains the hallmark features of protein kinases, whereas the COOH-terminus is rich in proline and glutamine. Mutations in HRR25 at conserved residues found in all protein kinases inactivated the gene, and these mutants exhibited the hrr25 null phenotypes. Taken together, the hrr25 mutant phenotypes and the features of the gene product indicate that HRR25 is a distinctive member of the protein kinase superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoekstra, M F -- Liskay, R M -- Ou, A C -- DeMaggio, A J -- Burbee, D G -- Heffron, F -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1031-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Casein Kinase I ; *DNA Damage ; *DNA Repair ; Fungal Proteins/*genetics/metabolism ; Gene Library ; Genes, Fungal ; Meiosis ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Phenotype ; *Protein Kinases ; Restriction Mapping ; Saccharomyces cerevisiae/enzymology/*genetics/physiology ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid
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  • 20
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    Control of alternative splicing by the differential binding of U1 small nuclear ribonucleoprotein particle (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: Cellular factors controlling alternative splicing of precursor messenger RNA are largely unknown, even though this process plays a central role in specifying the diversity of proteins in the eukaryotic cell. For the identification of such factors, a segment of the rat preprotachykinin gene was used in which differential expression of neuropeptides gamma and K is dependent on alternative splicing of the fourth exon (E4). Sequence variants of the three-exon segment, (E3-E4-E5) were created, resulting in a sensitive assay for factors mediating the splicing switch between E4-skipping and E4-inclusion. A dinucleotide mutation in the 5' splice site of E4 that increase base-pairing of this site to U1 small nuclear RNA resulted in uniform selection of E4, whereas a control mutation that destroyed base-pairing resulted in uniform E4-skipping. Affinity selection of spliceosomes formed on these functionally distinct substrates revealed that the extreme difference in splicing was mediated by differential binding of the U1 small nuclear ribonucleoprotein particle (snRNP) to the 5' splice site of E4. These data show that, apart from its established role in selecting 5' splice sites, U1 snRNP plays a fundamental role in 3' exon selection and provides insight into possible mechanisms of alternative splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuo, H C -- Nasim, F H -- Grabowski, P J -- GM-39695/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1045-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Brown University, Providence, RI 02912.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1825520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Mutational Analysis ; Exons ; Hydrogen Bonding ; Macromolecular Substances ; Molecular Sequence Data ; Protein Precursors/*genetics ; *RNA Splicing ; RNA, Messenger/*metabolism ; RNA, Small Nuclear/*physiology ; Rats ; Ribonucleoproteins/chemistry/*physiology ; Ribonucleoproteins, Small Nuclear ; Structure-Activity Relationship ; Tachykinins/*genetics
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  • 21
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    Translational potentiation of messenger RNA with secondary structure in Xenopus (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-15
    Description: Differential translation of messenger RNA (mRNA) with stable secondary structure in the 5' untranslated leader may contribute to the dramatic changes in protein synthetic patterns that occur during oogenesis and early development. Plasmids that contained the bacterial gene chloramphenicol acetyltransferase and which encoded mRNA with (hpCAT) or without (CAT) a stable hairpin secondary structure in the 5' noncoding region were transcribed in vitro, and the resulting mRNAs were injected into Xenopus oocytes, eggs, and early embryos. During early oogenesis, hpCAT mRNA was translated at less than 3 percent of the efficiency of CAT mRNA. The relative translational potential of hpCAT reached 100 percent in the newly fertilized egg and returned to approximately 3 percent after the midblastula transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, L N -- Ye, R Q -- Browder, L W -- Johnston, R N -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):807-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Calgary, Alberta, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990443" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chloramphenicol O-Acetyltransferase/genetics ; Egg Proteins/biosynthesis/genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oogenesis/genetics ; Plasmids ; *Protein Biosynthesis ; RNA, Messenger/*genetics ; Xenopus laevis/embryology/*genetics
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  • 22
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    Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-26
    Description: Malignant hyperthermia (MH) causes neurological, liver, and kidney damage and death in humans and major economic losses in the swine industry. A single point mutation in the porcine gene for the skeletal muscle ryanodine receptor (ryr1) was found to be correlated with MH in five major breeds of lean, heavily muscled swine. Haplotyping suggests that the mutation in all five breeds has a common origin. Assuming that this is the causal mutation for MH, the development of a noninvasive diagnostic test will provide the basis for elimination of the MH gene or its controlled inclusion in swine breeding programs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujii, J -- Otsu, K -- Zorzato, F -- de Leon, S -- Khanna, V K -- Weiler, J E -- O'Brien, P J -- MacLennan, D H -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862346" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Codon/genetics ; Haplotypes ; Malignant Hyperthermia/genetics/*veterinary ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Receptors, Cholinergic/*genetics ; Restriction Mapping ; Ryanodine/metabolism ; Ryanodine Receptor Calcium Release Channel ; Species Specificity ; Swine ; Swine Diseases/*genetics
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  • 23
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    Cloning of a factor required for activity of the Ah (dioxin) receptor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-17
    Description: The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E C -- Reyes, H -- Chu, F F -- Sander, F -- Conley, L H -- Brooks, B A -- Hankinson, O -- CA 16048/CA/NCI NIH HHS/ -- CA 28868/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1852076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytosol/metabolism ; *DNA-Binding Proteins ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Proteins/*genetics/metabolism ; RNA, Messenger/genetics ; Receptors, Aryl Hydrocarbon ; Receptors, Drug/genetics/*metabolism ; Sequence Homology, Nucleic Acid ; Tetrachlorodibenzodioxin/*metabolism ; *Transcription Factors ; Transfection
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  • 24
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    Specific DNA binding by c-Myb: evidence for a double helix-turn-helix-related motif (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-06
    Description: The c-Myb protein is a sequence-specific DNA binding protein that activates transcription in hematopoietic cells. Three imperfect repeats (R1, R2, and R3) that contain regularly spaced tryptophan residues form the DNA binding domain of c-Myb. A fragment of c-Myb that contained the R2 and R3 regions bound specifically to a DNA sequence recognized by c-Myb plus ten additional base pairs at the 3' end of the element. The R2R3 fragment was predicted to contain two consecutive helix-turn-helix (HTH) motifs with unconventional turns. Mutagenesis of amino acids in R2R3 at positions that correspond to DNA-contacting amino acids in other HTH-containing proteins abolished specific DNA binding without affecting nonspecific DNA interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrielsen, O S -- Sentenac, A -- Fromageot, P -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Ingenierie des Proteines, Centre d'Etudes de Saclay, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887237" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Oncogenes ; Polymerase Chain Reaction ; Protein Conformation ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-myb ; Recombinant Proteins/metabolism ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Transcription Factors/*metabolism
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  • 25
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    GRAIL seeks out genes buried in DNA sequence (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948063" target="_blank"〉PubMed〈/a〉
    Keywords: *Artificial Intelligence ; Base Sequence ; DNA/*genetics ; *Genes ; *Genome, Human ; Humans ; Molecular Sequence Data ; Software
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  • 26
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    Triplex DNA finally comes of age (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1374-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047850" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; DNA Replication ; Genes, myc ; Models, Molecular ; Molecular Sequence Data ; Transcription, Genetic/drug effects
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  • 27
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    Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-01
    Description: Apolipoprotein AI (apoAI) is a lipid-binding protein that participates in the transport of cholesterol and other lipids in the plasma. A complementary DNA clone for a protein that bound to regulatory elements of the apoAI gene was isolated. This protein, designated apoAI regulatory protein-1 (ARP-1), is a novel member of the steroid hormone receptor superfamily. ARP-1 bound to DNA as a dimer, and its dimerization domain was localized to the COOH-terminal region. ARP-1 also bound to a thyroid hormone-responsive element and to regulatory regions of the apoB, apoCIII, insulin, and ovalbumin genes. In cotransfection experiments, ARP-1 downregulated the apoAI gene. The involvement of ARP-1 in the regulation of apoAI gene expression suggests that it may participate in lipid metabolism and cholesterol homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ladias, J A -- Karathanasis, S K -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):561-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1899293" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoprotein A-I ; Apolipoproteins A/*genetics ; Base Sequence ; COUP Transcription Factor II ; COUP Transcription Factors ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation ; Humans ; Lipoproteins, HDL/*genetics ; Molecular Sequence Data ; Oligonucleotide Probes ; Receptors, Steroid/*metabolism ; Regulatory Sequences, Nucleic Acid ; *Transcription Factors
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    Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-29
    Description: Human immunodeficiency virus type 1 (HIV-1) gene expression is activated by Tat, a virally encoded protein. Tat trans-activation requires viral (trans-activation--responsive; TAR) RNA sequences located in the R region of the long terminal repeat (LTR). Existing evidence suggests that Tat probably cooperates with cellular factors that bind to TAR RNA in the overall trans-activation process. A HeLa complementary DNA was isolated and characterized that encodes a TAR RNA-binding protein (TRBP). TRBP activated the HIV-1 LTR and was synergistic with Tat function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatignol, A -- Buckler-White, A -- Berkhout, B -- Jeang, K T -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1597-600.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011739" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Carrier Proteins/*genetics ; Endoribonucleases/genetics ; Escherichia coli/enzymology ; *Escherichia coli Proteins ; Gene Products, tat/metabolism ; *HIV Long Terminal Repeat ; HIV-1/*genetics ; Humans ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmids ; RNA, Viral/genetics ; *RNA-Binding Proteins ; Ribonuclease III ; Sequence Homology, Nucleic Acid ; tat Gene Products, Human Immunodeficiency Virus
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    Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: Analysis of the heteromeric DNA binding protein GABP has revealed the interaction of two distinct peptide sequence motifs normally associated with proteins located in different cellular compartments. The alpha subunit of GABP contains an 85-amino acid segment related to the Ets family of DNA binding proteins. The ETS domain of GABP alpha facilitates weak binding to DNA and, together with an adjacent segment of 37 amino acids, mediates stable interaction with GABP beta. The beta subunit of GABP contains four imperfect repeats of a sequence present in several transmembrane proteins including the product of the Notch gene of Drosophila melanogaster. These amino-terminal repeats of GABP beta mediate stable interaction with GABP alpha and, when complexed with GABP alpha, directly contact DNA. These observations provide evidence for a distinct biochemical role for the 33-amino acid repeats, and suggest that they may serve as a module for the generation of specific dimerization interfaces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C C -- Brown, T A -- McKnight, S L -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):762-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Carnegie Institution of Washington, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cross-Linking Reagents ; DNA/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; GA-Binding Protein Transcription Factor ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Multigene Family ; Nuclear Proteins/*chemistry/metabolism ; Oligonucleotides/chemistry ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-ets ; Rats ; Recombinant Proteins ; Structure-Activity Relationship ; Transcription Factors/*chemistry/metabolism
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    Cell-free, de novo synthesis of poliovirus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: Cell-free translation of poliovirus RNA in an extract of uninfected human (HeLa) cells yielded viral proteins through proteolysis of the polyprotein. In the extract, newly synthesized proteins catalyzed poliovirus-specific RNA synthesis, and formed infectious poliovirus de novo. Newly formed virions were neutralized by type-specific antiserum, and infection of human cells with them was prevented by poliovirus receptor-specific antibodies. Poliovirus synthesis was increased nearly 70-fold when nucleoside triphosphates were added, but it was abolished in the presence of inhibitors of translation or viral genome replication. The ability to conduct cell-free synthesis of poliovirus will aid in the study of picornavirus proliferation and in the search for the control of picornaviral disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molla, A -- Paul, A V -- Wimmer, E -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1647-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, School of Medicine, State University of New York, Stony Brook 11794.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661029" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell-Free System ; HeLa Cells ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides/chemistry ; Poliovirus/*growth & development ; Polymerase Chain Reaction ; RNA, Viral/analysis/biosynthesis ; Time Factors ; Viral Proteins/biosynthesis/chemistry ; *Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    New role found for a common protein "motif" (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):742.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1831563" target="_blank"〉PubMed〈/a〉
    Keywords: Ankyrins ; Base Sequence ; Binding Sites ; Blood Proteins/*chemistry ; Membrane Proteins/*chemistry ; Molecular Sequence Data ; *Protein Binding ; Structure-Activity Relationship ; Transcription Factors/chemistry
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    Finding DNA sequencing errors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1255-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925537" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Dna ; Databases, Factual/*standards ; Humans ; National Library of Medicine (U.S.) ; Software ; United States
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  • 33
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    Oligoclonal expansion and CD1 recognition by human intestinal intraepithelial lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-20
    Description: A human intestinal intraepithelial lymphocyte (IEL) T cell line was established from jejunum to characterize the structure and function of the alpha beta T cell antigen receptors (TCRs) expressed by this population. Single-sided polymerase chain reaction (PCR) amplification cloning and quantitative PCR amplification of the TCR chains from the cell line and from fresh IELs demonstrated that IELs were oligoclonal. The IEL T cell line exhibited CD1-specific cytotoxicity and a dominant IEL T cell clone was CD1c-specific. Thus, human jejunal intraepithelial lymphocytes are oligoclonal and recognize members of the CD1 gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balk, S P -- Ebert, E C -- Blumenthal, R L -- McDermott, F V -- Wucherpfennig, K W -- Landau, S B -- Blumberg, R S -- 5 KO8 DK01886/DK/NIDDK NIH HHS/ -- CA-01310/CA/NCI NIH HHS/ -- DK42166/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1411-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hematology-Oncology Division, Beth Israel Hospital, Harvard Medical School, Boston, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD/*genetics/immunology ; Antigens, CD1 ; Base Sequence ; Cell Line ; Clone Cells ; Epithelium/physiology ; Humans ; Jejunum/immunology ; Molecular Sequence Data ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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    Conserved sequence and structural elements in the HIV-1 principal neutralizing determinant: corrections and clarifications (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaRosa, G J -- Davide, J P -- Weinhold, K -- Waterbury, J A -- Profy, A T -- Lewis, J A -- Langlois, A J -- Dreesman, G R -- Boswell, R N -- Shadduck, P -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):811.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; HIV-1/*genetics ; Molecular Sequence Data
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    FTZ-F1, a steroid hormone receptor-like protein implicated in the activation of fushi tarazu (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-10
    Description: The Drosophila homeobox segmentation gene fushi tarazu (ftz) is expressed in a seven-stripe pattern during early embryogenesis. This characteristic pattern is largely specified by the zebra element located immediately upstream of the ftz transcriptional start site. The FTZ-F1 protein, one of multiple DNA binding factors that interacts with the zebra element, is implicated in the activation of ftz transcription, especially in stripes 1, 2, 3, and 6. An FTZ-F1 complementary DNA has been cloned by recognition site screening of a Drosophila expression library. The identity of the FTZ-F1 complementary DNA clone was confirmed by immunological cross-reaction with antibodies to FTZ-F1 and by sequence analysis of peptides from purified FTZ-F1 protein. The predicted amino acid sequence of FTZ-F1 revealed that the protein is a member of the nuclear hormone receptor superfamily. This finding raises the possibility that a hormonal ligand affects the expression of a homeobox segmentation gene early in embryonic development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lavorgna, G -- Ueda, H -- Clos, J -- Wu, C -- New York, N.Y. -- Science. 1991 May 10;252(5007):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Blotting, Southern ; Blotting, Western ; Chromosome Mapping ; Cloning, Molecular ; Drosophila Proteins ; Drosophila melanogaster ; Fushi Tarazu Transcription Factors ; Gene Expression Regulation ; Genes, Homeobox ; *Homeodomain Proteins ; Insect Hormones/*chemistry ; Molecular Sequence Data ; Open Reading Frames ; RNA/analysis ; Receptors, Steroid/genetics ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Zinc Fingers
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    Tissue-specific splicing in vivo of the beta-tropomyosin gene: dependence on an RNA secondary structure (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-28
    Description: The beta-tropomyosin gene in chicken contains two mutually exclusive exons (exons 6A and 6B) which are used by the splicing apparatus in myogenic cells, respectively, before (myoblast stage) and after (myotube stage) differentiation. The myoblast splicing pattern is shown to depend on multiple sequence elements that are located in the upstream intron and in the exon 6B and that exert a negative control over exon 6B splicing. This regulation of splicing is due, at least in part, to a secondary structure of the primary transcript, which limits in vivo the accessibility of exon 6B in myoblasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Libri, D -- Piseri, A -- Fiszman, M Y -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1842-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063196" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Exons ; Introns ; Models, Molecular ; Molecular Sequence Data ; Muscles/physiology ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; RNA Precursors/*genetics ; *RNA Splicing ; RNA, Messenger/*genetics ; Transcription, Genetic ; Tropomyosin/*genetics
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    Functional contribution of neuronal AChR subunits revealed by antisense oligonucleotides (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-06
    Description: Although multiple related genes encoding nicotinic acetylcholine receptor (AChR) subunits have been identified, how each of these subunits contributes to AChRs in neurons is not known. Sympathetic neurons express four classes of AChR channels and six AChR subunit genes (alpha 3, alpha 4, alpha 5, alpha 7, beta 2, and beta 4). The contribution of individual subunits to AChR channel subtypes in these neurons was examined by selective deletion with antisense oligonucleotides. An alpha 3 antisense oligonucleotide decreased the number and altered the properties of the normally expressed ACh-activated channels. The remaining AChR channels have distinct biophysical and pharmacological properties that indicate an important functional contribution of the alpha 7 subunit.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2366811/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2366811/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Listerud, M -- Brussaard, A B -- Devay, P -- Colman, D R -- Role, L W -- NS 29071/NS/NINDS NIH HHS/ -- NS27680/NS/NINDS NIH HHS/ -- R01 NS029071/NS/NINDS NIH HHS/ -- R01 NS029071-09/NS/NINDS NIH HHS/ -- R01 NS029071-10/NS/NINDS NIH HHS/ -- R01 NS029071-11/NS/NINDS NIH HHS/ -- R01 NS029071-12/NS/NINDS NIH HHS/ -- R01 NS029071-13/NS/NINDS NIH HHS/ -- R01 NS029071-13S1/NS/NINDS NIH HHS/ -- R01 NS029071-14/NS/NINDS NIH HHS/ -- R01 NS029071-15/NS/NINDS NIH HHS/ -- R01 NS029071-16/NS/NINDS NIH HHS/ -- R01 NS029071-17/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Columbia College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bungarotoxins/pharmacology ; Chick Embryo ; Gene Expression ; Ion Channel Gating ; Ion Channels/*physiology ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Receptors, Nicotinic/*physiology/ultrastructure ; Structure-Activity Relationship ; Sympathetic Nervous System/*physiology
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    Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-08
    Description: The myc protooncogene family has been implicated in cell proliferation, differentiation, and neoplasia, but its mechanism of function at the molecular level is unknown. The carboxyl terminus of Myc family proteins contains a basic region helix-loop-helix leucine zipper motif (bHLH-Zip), which has DNA-binding activity and has been predicted to mediate protein-protein interactions. The bHLH-Zip region of c-Myc was used to screen a complementary DNA (cDNA) expression library, and a bHLH-Zip protein, termed Max, was identified. Max specifically associated with c-Myc, N-Myc, and L-Myc proteins, but not with a number of other bHLH, bZip, or bHLH-Zip proteins. The interaction between Max and c-Myc was dependent on the integrity of the c-Myc HLH-Zip domain, but not on the basic region or other sequences outside the domain. Furthermore, the Myc-Max complex bound to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibited appreciable binding. The DNA-binding activity of the complex was dependent on both the dimerization domain and the basic region of c-Myc. These results suggest that Myc family proteins undergo a restricted set of interactions in the cell and may belong to the more general class of eukaryotic DNA-binding transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blackwood, E M -- Eisenman, R N -- P01 CA28151/CA/NCI NIH HHS/ -- R01 CA20525/CA/NCI NIH HHS/ -- T32 CA09437/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1211-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Cloning, Molecular ; DNA-Binding Proteins/*genetics/metabolism ; Escherichia coli/genetics ; Gene Library ; *Genes, myc ; Glutathione Transferase/genetics/metabolism ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes ; Protein Biosynthesis ; Proto-Oncogene Proteins c-myc/*genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; *Transcription Factors ; Transcription, Genetic
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    Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: The neurotransmitter serotonin (5HT) activates a variety of second messenger signaling systems and through them indirectly regulates the function of ion channels. Serotonin also activates ion channels directly, suggesting that it may also mediate rapid, excitatory responses. A complementary DNA clone containing the coding sequence of one of these rapidly responding channels, a 5HT3 subtype of the serotonin receptor, has been isolated by screening a neuroblastoma expression library for functional expression of serotonin-gated currents in Xenopus oocytes. The predicted protein product has many of the features shared by other members of the ligand-gated ion channel family. The pharmacological and electrophysiological characteristics of the cloned receptor are largely consistent with the properties of native 5HT3 receptors. Messenger RNA encoding this receptor is found in the brain, spinal cord, and heart. This receptor defines a new class of excitatory ligand-gated channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maricq, A V -- Peterson, A S -- Brake, A J -- Myers, R M -- Julius, D -- GM44298/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):432-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143-0450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718042" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cell Line ; Ion Channels/*chemistry/drug effects/physiology ; Mice ; Molecular Sequence Data ; Oocytes/metabolism ; Poly A ; RNA, Messenger ; Radioligand Assay ; Receptors, Serotonin/*chemistry/drug effects/physiology ; Xenopus
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    Variable effects of phosphorylation of Pit-1 dictated by the DNA response elements (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: Pit-1, a tissue-specific POU domain transcription factor, is required for the activation of the prolactin, growth hormone, and Pit-1 promoters that confer regulation by epidermal growth factor, adenosine 3',5'-monophosphate (cAMP), and phorbol esters. Pit-1 is phosphorylated in pituitary cells at two distinct sites in response to phorbol esters and cAMP. Phosphorylation of Pit-1 modifies its conformation on DNA recognition elements and results in increased binding at certain sites and decreased binding at other sites, dependent on DNA sequences adjacent to the core Pit-1 binding motif. One residue (Thr220), located in the POU homeodomain within a sequence conserved throughout the POU-domain family, confers these responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kapiloff, M S -- Farkash, Y -- Wegner, M -- Rosenfeld, M G -- DK 18477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):786-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Regulatory Biology Program, School of Medicine, University of California, San Diego, La Jolla 92093-0648.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1652153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cell Line ; Cyclic AMP/pharmacology ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*physiology ; In Vitro Techniques ; Molecular Sequence Data ; Peptide Mapping ; Phosphorylation ; Phosphothreonine/metabolism ; Pituitary Gland/*physiology ; Protein Kinases/metabolism ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/*physiology ; Trypsin
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    Sigma factor relatives in eukaryotes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaehning, J A -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):859.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876846" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/genetics ; *Eukaryotic Cells ; Humans ; Molecular Sequence Data ; RNA Polymerase II/metabolism ; Sequence Homology, Nucleic Acid ; Sigma Factor/genetics/*metabolism ; Transcription Factors/genetics/*metabolism
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  • 42
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    Long-range structure in ribonuclease P RNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA. This feature strongly constrains the three-dimensional structure of RNase P RNA near the active site. Some RNase P RNAs lack this structure but contain a unique, possibly compensating, structural domain. This suggests that different RNA structures located at different positions in the sequence may have equivalent architectural functions in RNase P RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haas, E S -- Morse, D P -- Brown, J W -- Schmidt, F J -- Pace, N R -- GM34527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719634" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/enzymology/genetics ; Base Composition ; Base Sequence ; Biological Evolution ; Endoribonucleases/*genetics ; Escherichia coli/enzymology/genetics ; *Escherichia coli Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Conformation ; RNA, Bacterial/*genetics ; RNA, Catalytic/*genetics ; Ribonuclease P
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  • 43
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    Deleted HTLV-I provirus in blood and cutaneous lesions of patients with mycosis fungoides (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-19
    Description: Mycosis fungoides, a rare form of cutaneous T cell leukemia/lymphoma, is suspected of having a viral etiology on the basis of certain similarities to adult T cell leukemia, which is associated with human T cell leukemia/lymphoma virus type I (HTLV-I) infection. Cell lines were established from peripheral blood mononuclear cells (PBMC) of an HTLV-I-seronegative patient with mycosis fungoides. DNA hybridization analysis revealed the presence of HTLV-I-related sequences with unusual restriction endonuclease sites. Sequence analysis of subcloned fragments demonstrated the presence of a monoclonally integrated provirus with a 5.5-kilobase deletion involving large regions of gag and env and all of pol. Additional evidence for the presence of deleted proviruses was found by polymerase chain reaction (PCR) amplification of DNA from cutaneous lesions of five other HTLV-I-seronegative patients. The findings suggest that HTLV-I infection may be involved in the etiology of at least certain cases of mycosis fungoides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, W W -- Liu, C R -- Schneewind, O -- Takahashi, H -- Kaplan, M H -- Roupe, G -- Vahlne, A -- CA51012-01A1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Disease, North Shore University Hospital-Cornell University Medical College, Manhasset, NY 11030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857968" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosome Deletion ; DNA, Neoplasm/genetics/isolation & purification ; DNA, Viral/genetics/isolation & purification ; *Genes, Viral ; Human T-lymphotropic virus 1/genetics/*isolation & purification ; Humans ; Lymphocytes/*microbiology ; Molecular Sequence Data ; Mycosis Fungoides/blood/*microbiology ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Proviruses/genetics/*isolation & purification ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Skin/*microbiology ; Skin Neoplasms/blood/*microbiology
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  • 44
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    The human genome initiative--do databases reflect current progress? (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, P L -- Maidak, B -- Chipperfield, M -- Robbins, R -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):214-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Welch Lab for Applied Research in Academic Information, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925578" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Databases, Factual ; Genome, Human ; *Human Genome Project ; Humans
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  • 45
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    Kinetic characterization of ribonuclease-resistant 2'-modified hammerhead ribozymes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-19
    Description: The incorporation of 2'-fluoro- and 2'-aminonucleotides into a hammerhead ribozyme was accomplished by automated chemical synthesis. The presence of 2'-fluorouridines, 2'-fluorocytidines, or 2'-aminouridines did not appreciably decrease catalytic efficiency. Incorporation of 2'-aminocytidines decreased ribozyme activity approximately by a factor of 20. The replacement of all adenosines with 2'-fluoroadenosines abolished catalysis in the presence of MgCl2 within the limits of detection, but some activity was retained in the presence of MnCl2. This effect on catalysis was localized to a specific group of adenines within the conserved single-stranded region of the ribozyme. The decrease in catalytic efficiency was caused by a decrease in the rate constant; the Michaelis constant was unaltered. The 2'-fluoro and 2'-amino modifications conferred resistance toward ribonuclease degradation. Ribozymes containing 2'-fluoro- or 2'-aminonucleotides at all uridine and cytidine positions were stabilized against degradation in rabbit serum by a factor of at least 10(3) compared to unmodified ribozyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pieken, W A -- Olsen, D B -- Benseler, F -- Aurup, H -- Eckstein, F -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):314-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Experimentelle Medizin, Abteilung Chemie, Gottingen, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857967" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chlorides ; Kinetics ; Magnesium Chloride/pharmacology ; Manganese/pharmacology ; *Manganese Compounds ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/chemical synthesis/*metabolism ; Ribonucleases/*metabolism ; Ribonucleotides ; Substrate Specificity
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  • 46
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    Identification of a gene located at chromosome 5q21 that is mutated in colorectal cancers (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-15
    Description: Recent studies have suggested the existence of a tumor suppressor gene located at chromosome region 5q21. DNA probes from this region were used to study a panel of sporadic colorectal carcinomas. One of these probes, cosmid 5.71, detected a somatically rearranged restriction fragment in the DNA from a single tumor. Further analysis of the 5.71 cosmid revealed two regions that were highly conserved in rodent DNA. These sequences were used to identify a gene, MCC (mutated in colorectal cancer), which encodes an 829-amino acid protein with a short region of similarity to the G protein-coupled m3 muscarinic acetylcholine receptor. The rearrangement in the tumor disrupted the coding region of the MCC gene. Moreover, two colorectal tumors were found with somatically acquired point mutations in MCC that resulted in amino acid substitutions. MCC is thus a candidate for the putative colorectal tumor suppressor gene located at 5q21. Further studies will be required to determine whether the gene is mutated in other sporadic tumors or in the germ line of patients with an inherited predisposition to colonic tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinzler, K W -- Nilbert, M C -- Vogelstein, B -- Bryan, T M -- Levy, D B -- Smith, K J -- Preisinger, A C -- Hamilton, S R -- Hedge, P -- Markham, A -- 6M 07184/PHS HHS/ -- CA 06973/CA/NCI NIH HHS/ -- CA 09243/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1366-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Genetics Laboratory, Johns Hopkins Oncology Center, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848370" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; *Chromosomes, Human, Pair 5 ; Colorectal Neoplasms/*genetics ; Exons ; GTP-Binding Proteins/metabolism ; Gene Expression ; *Genes, Tumor Suppressor ; Humans ; Molecular Sequence Data ; Mutation ; Oligonucleotides/chemistry ; Polymerase Chain Reaction ; Proteins/*genetics/metabolism ; Rats ; Sequence Homology, Nucleic Acid ; *Tumor Suppressor Proteins
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  • 47
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    Regulation of a segmentation stripe by overlapping activators and repressors in the Drosophila embryo (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: Gene expression stripes in Drosophila melanogaster embryos provide a model for how eukaryotic promoters are turned on and off in response to combinations of transcriptional regulators. Genetic studies suggested that even-skipped (eve) stripe 2 is controlled by three gap genes, hunchback (hb), Kruppel (Kr), and giant (gt), and by the maternal morphogen bicoid (bcd). A direct link is established between binding sites for these regulatory proteins in the stripe 2 promoter element and the expression of the stripe during early embryogenesis. The bcd and hb protein binding sites mediate activation, whereas neighboring gt and Kr protein sites repress expression and establish the stripe borders. The stripe 2 element has the properties of a genetic on-off switch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stanojevic, D -- Small, S -- Levine, M -- GM 34431/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1385-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Fairchild Center, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1683715" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Deletion ; Drosophila melanogaster/embryology/*genetics ; Embryo, Nonmammalian/physiology ; Gene Expression Regulation ; *Genes ; Genes, Homeobox ; Molecular Sequence Data ; Morphogenesis ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Promoter Regions, Genetic
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    Suppression of the immune response by a soluble complement receptor of B lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: The CD19-CR2 complex of B lymphocytes contains proteins that participate in two host-defense systems, the immune and complement systems. The ligand for the subunit of the immune system, CD19, is not known, but the complement receptor subunit, CR2 (CD21), binds activation fragments of the C3 component of the complement system and may mediate immunopotentiating effects of complement. A recombinant, soluble CR2 was prepared by fusing the C3-binding region of the receptor to immunoglobulin G1 (IgG1). The (CR2)2-IgG1 chimera competed with cellular CR2 for C3 binding and suppressed the antibody response to a T cell-dependent antigen when administered to mice at the time of immunization. This inhibitory effect of (CR2)2-IgG1 demonstrates the B cell-activating function of the CD19-CR2 complex and suggests a new method for humoral immunosuppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hebell, T -- Ahearn, J M -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- GM-43803/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antibody Formation ; Antigens, CD/*physiology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/chemistry/*physiology ; B-Lymphocytes/*physiology ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; Immunosuppression ; In Vitro Techniques ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Receptors, Complement/chemistry/*physiology ; Receptors, Complement 3d ; Recombinant Fusion Proteins ; Signal Transduction ; Solubility
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  • 49
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    Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The nucleotides crucial for the specific aminoacylation of yeast tRNA(Asp) by its cognate synthetase have been identified. Steady-state aminoacylation kinetics of unmodified tRNA transcripts indicate that G34, U35, C36, and G73 are important determinants of tRNA(Asp) identity. Mutations at these positions result in a large decrease (19- to 530-fold) of the kinetic specificity constant (ratio of the catalytic rate constant kcat and the Michaelis constant Km) for aspartylation relative to wild-type tRNA(Asp). Mutation to G10-C25 within the D-stem reduced kcat/Km eightfold. This fifth mutation probably indirectly affects the presentation of the highly conserved G10 nucleotide to the synthetase. A yeast tRNA(Phe) was converted into an efficient substrate for aspartyl-tRNA synthetase through introduction of the five identity elements. The identity nucleotides are located in regions of tight interaction between tRNA and synthetase as shown in the crystal structure of the complex and suggest sites of base-specific contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Putz, J -- Puglisi, J D -- Florentz, C -- Giege, R -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biochimie, Institut de Biologie Moleculaire et Cellulaire du CNRS, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047878" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartate-tRNA Ligase/*metabolism ; Base Sequence ; Computer Graphics ; DNA Mutational Analysis ; Fungal Proteins/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; RNA, Fungal/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; RNA, Transfer, Asp/*metabolism ; Saccharomyces cerevisiae/*enzymology ; Structure-Activity Relationship ; Substrate Specificity ; *Transfer RNA Aminoacylation
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    Toward cloning and mapping the genome of Drosophila (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-11
    Description: An ultimate goal of Drosophila genetics is to identify and define the functions of all the genes in the organism. Traditional approaches based on the isolation of mutant genes have been extraordinary fruitful. Recent advances in the manipulation and analysis of large DNA fragments have made it possible to develop detailed molecular maps of the Drosophila genome as the initial steps in determining the complete DNA sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merriam, J -- Ashburner, M -- Hartl, D L -- Kafatos, F C -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925579" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; *Chromosome Mapping ; Chromosomes ; *Cloning, Molecular ; Drosophila melanogaster/*genetics ; Gene Rearrangement ; Genes ; *Genome ; Mutation
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    Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-23
    Description: FK506 and rapamycin are related immunosuppressive compounds that block helper T cell activation by interfering with signal transduction. In vitro, both drugs bind and inhibit the FK506-binding protein (FKBP) proline rotamase. Saccharomyces cerevisiae cells treated with rapamycin irreversibly arrested in the G1 phase of the cell cycle. An FKBP-rapamycin complex is concluded to be the toxic agent because (i) strains that lack FKBP proline rotamase, encoded by FPR1, were viable and fully resistant to rapamycin and (ii) FK506 antagonized rapamycin toxicity in vivo. Mutations that conferred rapamycin resistance altered conserved residues in FKBP that are critical for drug binding. Two genes other than FPR1, named TOR1 and TOR2, that participate in rapamycin toxicity were identified. Nonallelic noncomplementation between FPR1, TOR1, and TOR2 alleles suggests that the products of these genes may interact as subunits of a protein complex. Such a complex may mediate nuclear entry of signals required for progression through the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitman, J -- Movva, N R -- Hall, M N -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):905-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/metabolism/pharmacology ; Base Sequence ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/chemistry/genetics/metabolism ; Cell Cycle/*drug effects ; Cyclosporins/pharmacology ; Drug Resistance, Microbial/genetics ; G1 Phase/drug effects ; Humans ; Immunosuppressive Agents/pharmacology ; Molecular Sequence Data ; Molecular Structure ; Mutation ; Polyenes/metabolism/*pharmacology ; Saccharomyces cerevisiae/*cytology/drug effects ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Sirolimus ; Tacrolimus ; Tacrolimus Binding Proteins
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    Site-specific cleavage of human chromosome 4 mediated by triple-helix formation (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Direct physical isolation of specific DNA segments from the human genome is a necessary goal in human genetics. For testing whether triple-helix mediated enzymatic cleavage can liberate a specific segment of a human chromosome, the tip of human chromosome 4, which contains the entire candidate region for the Huntington's disease gene, was chosen as a target. A 16-base pyrimidine oligodeoxyribonucleotide was able to locate a 16-base pair purine target site within more than 10 gigabase pairs of genomic DNA and mediate the exact enzymatic cleavage at that site in more than 80 percent yield. The recognition motif is sufficiently generalizable that most cosmids should contain a sequence targetable by triple-helix formation. This method may facilitate the orchestrated dissection of human chromosomes from normal and affected individuals into megabase sized fragments and facilitate the isolation of candidate gene loci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strobel, S A -- Doucette-Stamm, L A -- Riba, L -- Housman, D E -- Dervan, P B -- HG00098/HG/NHGRI NIH HHS/ -- HG00329/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1639-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arnold and Mabel Beckman Laboratories of Chemical Synthesis, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1836279" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping/methods ; Chromosomes, Human, Pair 4/*ultrastructure ; DNA Damage ; Humans ; Huntington Disease/genetics ; Hydrogen Bonding ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry ; Restriction Mapping
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    Isolation of sequences that span the fragile X and identification of a fragile X-related CpG island (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-08
    Description: Yeast artificial chromosomes (YACs) were obtained from a 550-kilobase region that contains three probes previously mapped as very close to the locus of the fragile X syndrome. These YACs spanned the fragile site in Xq27.3 as shown by fluorescent in situ hybridization. An internal 200-kilobase segment contained four chromosomal breakpoints generated by induction of fragile X expression. A single CpG island was identified in the cloned region between markers DXS463 and DXS465 that appears methylated in mentally retarded fragile X males, but not in nonexpressing male carriers of the mutation nor in normal males. This CpG island may indicate the presence of a gene involved in the clinical phenotype of the syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitz, D -- Rousseau, F -- Devys, D -- Saccone, S -- Abderrahim, H -- Le Paslier, D -- Cohen, D -- Vincent, A -- Toniolo, D -- Della Valle, G -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1236-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, Institut de Chimie Biologique, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006411" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Fungal ; Cloning, Molecular ; DNA Probes ; *Dinucleoside Phosphates ; Fragile X Syndrome/*genetics ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Reference Values ; Restriction Mapping ; Saccharomyces cerevisiae/genetics ; *X Chromosome
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    Electronic data publishing and GenBank (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: GenBank, the national repository for nucleotide sequence data, has implemented a new model of scientific data management, which we term electronic data publishing. In traditional publishing, both scientific conclusions and supporting data are communicated via the printed page, and in electronic journal publishing, both types of information are communicated via electronic media. In electronic data publishing, by contrast, conclusions are published in a journal while data are published via a network-accessible, electronic database.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cinkosky, M J -- Fickett, J W -- Gilna, P -- Burks, C -- GM-7-2110/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1273-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, NM 87545.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925538" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; Data Collection/methods ; *Databases, Factual ; *Electronics ; Human Genome Project ; Humans ; *Publishing ; Software
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    Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-02
    Description: To determine the role of the BCR-ABL gene in the proliferation of blast cells of patients with chronic myelogenous leukemia, leukemia blast cells were exposed to synthetic 18-mer oligodeoxynucleotides complementary to two identified BCR-ABL junctions. Leukemia colony formation was suppressed, whereas granulocyte-macrophage colony formation from normal marrow progenitors was unaffected. When equal proportions of normal marrow progenitors and blast cells were mixed, exposed to the oligodeoxynucleotides, and assayed for residual colony formation, the majority of residual cells were normal. These findings demonstrate the requirement for a functional BCR-ABL gene in maintaining the leukemic phenotype and the feasibility of gene-targeted selective killing of neoplastic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szczylik, C -- Skorski, T -- Nicolaides, N C -- Manzella, L -- Malaguarnera, L -- Venturelli, D -- Gewirtz, A M -- Calabretta, B -- CA09644/CA/NCI NIH HHS/ -- CA36896/CA/NCI NIH HHS/ -- CA46782/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):562-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Temple University Medical School, Philadelphia, PA 19140.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857987" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blast Crisis/genetics/pathology ; Cell Division/drug effects ; Exons ; Fusion Proteins, bcr-abl/*genetics ; Gene Expression/drug effects ; Humans ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/genetics/*pathology ; Molecular Sequence Data ; Monocytes/cytology/drug effects ; Oligonucleotides, Antisense/*pharmacology ; *Oncogenes ; RNA, Messenger/analysis/genetics ; Tumor Cells, Cultured/cytology/drug effects ; Tumor Stem Cell Assay ; beta 2-Microglobulin/genetics
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    Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-18
    Description: The mechanism by which cell surface molecules regulate T cell production of lymphokines is poorly understood. Production of interleukin-2 (IL-2) can be regulated by signal transduction pathways distinct from those induced by the T cell antigen receptor. Stimulation of CD28, a molecule expressed on most human T cells, induced the formation of a protein complex that bound to a site on the IL-2 gene distinct from previously described binding sites and increased IL-2 enhancer activity fivefold. The CD28-responsive complex bound to the IL-2 gene between -164 and -154 base pairs from the transcription start site. The sequence of this element is similar to regions conserved in the 5' flanking regions of several other lymphokine genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, J D -- Irving, B A -- Crabtree, G R -- Weiss, A -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846244" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD28 ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; Cell Line ; DNA Mutational Analysis ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; In Vitro Techniques ; Interleukin-2/*genetics ; Molecular Sequence Data ; Oligonucleotides/chemistry ; *Regulatory Sequences, Nucleic Acid ; Signal Transduction ; T-Lymphocytes/*physiology ; Transcription, Genetic
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    Type-specific regulation of adenylyl cyclase by G protein beta gamma subunits (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)-bound alpha subunits and a complex of beta and gamma subunits after interaction with receptors. The GTP-alpha subunit complex activates appropriate effectors, such as adenylyl cyclase, retinal phosphodiesterase, phospholipase C, and ion channels. G protein beta gamma subunits have been found to have regulatory effects on certain types of adenylyl cyclase. In the presence of Gs alpha, the alpha subunit of the G protein that activates adenylyl cyclase, one form of adenylyl cyclase was inhibited by beta gamma, some forms were activated by beta gamma, and some forms were not affected by beta gamma. These interactions suggest mechanisms for communication between distinct signal-transducing pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, W J -- Gilman, A G -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1500-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962211" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/classification/genetics/*metabolism ; Animals ; Base Sequence ; Cattle ; Cloning, Molecular ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; Guanosine Triphosphate/physiology ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Rabbits ; Recombinant Proteins
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    RNA secondary structure repression of a muscle-specific exon in HeLa cell nuclear extracts (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: The chicken beta-tropomyosin pre-messenger RNA (pre-mRNA) is spliced in a tissue-specific manner to yield messenger RNA's (mRNA's) coding for different isoforms of this protein. Exons 6A and 6B are spliced in a mutually exclusive manner; exon 6B was included in skeletal muscle, whereas exon 6A was preferred in all other tissues. The distal portion of the intron upstream of exon 6B was shown to form stable double-stranded regions with part of the intron downstream of exon 6B and with sequences in exon 6B. This structure repressed splicing of exon 6B to exon 7 in a HeLa cell extract. Derepression of splicing occurred on disruption of this structure and repression followed when the structure was re-formed, even if the structure was formed between two different RNA molecules. Repression leads to inhibition of formation of spliceosomes. Disrupting either of the two double-stranded regions could lead to derepression, whereas re-forming the helices by suppressor mutations reestablished repression. These results support a simple model of tissue-specific splicing in this region of the pre-mRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clouet d'Orval, B -- d'Aubenton Carafa, Y -- Sirand-Pugnet, P -- Gallego, M -- Brody, E -- Marie, J -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1823-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Genetique Moleculaire, C.N.R.S., Universite de Paris VI, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063195" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/*physiology ; Chickens ; *Exons ; HeLa Cells/physiology ; Humans ; Introns ; Molecular Sequence Data ; Muscles/*physiology ; Nucleic Acid Conformation ; RNA Precursors/chemistry/*genetics ; RNA Splicing ; Tropomyosin/*genetics
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    Prevention of apoptosis by a baculovirus gene during infection of insect cells (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: Programmed cell death is an active process of self destruction that is important in both the development and maintenance of multicellular animals. The molecular mechanisms controlling activation or suppression of programmed cell death are largely unknown. Apoptosis, a morphologically and biochemically defined type of programmed cell death commonly seen in vertebrates, was found to be initiated during baculovirus replication in insect cells. A specific viral gene product, p35, was identified as being responsible for blocking the apoptotic response. Identification of the function of this gene will allow further definition of the molecular pathways involved in the regulation of programmed cell death and may identify the role of apoptosis in invertebrate viral defense systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clem, R J -- Fechheimer, M -- Miller, L K -- AI23719/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1388-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Georgia, Athens 30602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962198" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Baculoviridae/*genetics ; Base Sequence ; *Cell Death ; Cell Line ; *Genes, Viral ; Insects ; Molecular Sequence Data ; Mutagenesis, Insertional ; Open Reading Frames ; Phenotype ; Restriction Mapping
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    Prediction of a crystallization pathway for Z-DNA hexanucleotides (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-15
    Description: Crystallization of macromolecules for structural studies has long been a hit-or-miss process. The crystallization of hexanucleotides as Z-DNA was studied, and it was shown that the cation concentration for crystal formation could be predicted from solvation free energy (SFE) calculations. Solution studies on the conformation and solubilities of the hexanucleotides showed that a critical concentration of the DNA in the Z-conformation must be present in solution to effect crystallization. The SFE calculations therefore predict the propensity of the hexanucleotides to adopt the left-handed conformation and the driving force required to reach this critical concentration relative to the intrinsic solubility of Z-DNA for crystallization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, P S -- Kagawa, T F -- Tseng, K H -- Schroth, G P -- Zhou, G W -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1003-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948069" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cations ; Crystallography ; DNA/*chemistry/ultrastructure ; Models, Molecular ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemistry ; Spectrophotometry, Ultraviolet
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    Cloning of a serotonin transporter affected by antidepressants (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: A complementary DNA clone for a serotonin (5HT) transporter has been isolated from rat basophilic leukemia cells. The complementary DNA sequence predicts a 653-amino acid protein with 12 to 13 putative transmembrane domains. The 5HT transporter has significant homology to the gamma-aminobutyric acid, dopamine, and norepinephrine transporters. Uptake by CV-1 cells expressing the transporter complementary DNA resembles 5HT uptake by platelets and brain synaptosomes; it is sensitive to antidepressants, amphetamine derivatives, and cocaine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, B J -- Mezey, E -- Brownstein, M J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):579-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents/*pharmacology ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cloning, Molecular ; Kinetics ; Leukemia, Basophilic, Acute ; Molecular Sequence Data ; Oligonucleotide Probes ; Rats ; Serotonin/*metabolism ; Transfection
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    A dominant negative form of transcription activator mTFE3 created by differential splicing (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-04
    Description: Transcription factor E3 (mTFE3) is a murine transcription activator that binds to the intronic enhancer of the immunoglobulin heavy chain gene. A naturally occurring splice product of mTFE3 messenger RNA (mRNA) lacked 105 nucleotides that encode an activation domain; both absolute and relative amounts of long and truncated mRNAs varied in different tissues. Cells were cotransfected with complementary DNAs that encoded the two mRNA forms in amounts that corresponded to the amounts of each mRNA found in different cells. Small changes in substoichiometric amounts of the truncated form of mRNA effected trans-dominant negative modulation of mTFE3 activity. These findings identify a function for differential splicing in the regulation of transcription factor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roman, C -- Cohn, L -- Calame, K -- R01CA38571/CA/NCI NIH HHS/ -- R01GM28361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):94-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; DNA-Binding Proteins/*genetics ; *Gene Expression Regulation ; Mice ; Molecular Sequence Data ; RNA Splicing ; RNA, Messenger/genetics ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Transcription Factors/*genetics ; *Transcription, Genetic
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    Specificity for aminoacylation of an RNA helix: an unpaired, exocyclic amino group in the minor groove (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-16
    Description: An acceptor stem G3.U70 base pair is a major determinant of the identity of an alanine transfer RNA. Hairpin helices and RNA duplexes consisting of complementary single strands are aminoacylated with alanine if they contain G3.U70. Chemical synthesis of RNA duplexes enabled the introduction of base analogs that tested the role of specific functional groups in the major and minor grooves of the RNA helix. The results of these experiments indicate that an unpaired guanine 2-amino group at a specific position in the minor groove of an RNA helix marks a molecule for aminoacylation with alanine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Musier-Forsyth, K -- Usman, N -- Scaringe, S -- Doudna, J -- Green, R -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- GM37641/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):784-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876835" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alanine-tRNA Ligase/*metabolism ; Base Sequence ; In Vitro Techniques ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Oligonucleotides/chemistry ; RNA, Transfer, Ala/chemistry/*metabolism ; Structure-Activity Relationship
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    Rel-associated pp40: an inhibitor of the rel family of transcription factors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-23
    Description: The Rel-associated protein pp40 is functionally related to I kappa B, an inhibitor of the transcription factor NF-kappa B. Purified pp40 inhibits the DNA binding activity of the NF-kappa B protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian I kappa B-like activity. Protein sequencing of I kappa B purified from rabbit lung confirmed that MAD-3 encodes a protein similar to I kappa B. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, N -- Ghosh, S -- Simmons, D L -- Tempst, P -- Liou, H C -- Baltimore, D -- Bose, H R Jr -- CA09583/CA/NCI NIH HHS/ -- CA2616/CA/NCI NIH HHS/ -- CA33192/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891714" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA Probes ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotide Probes ; Oncogene Proteins v-rel ; Open Reading Frames ; Phosphoproteins/*genetics/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors ; RNA, Messenger/genetics ; Retroviridae Proteins, Oncogenic/*antagonists & inhibitors ; Sequence Homology, Nucleic Acid ; Transcription Factors/*antagonists & inhibitors
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    "Sequence-gazing?" (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckwith, J -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1161-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006404" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics ; Base Sequence ; Escherichia coli/*genetics ; *Genes, Bacterial ; *Open Reading Frames
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    Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 DNA binding activity (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-20
    Description: Oct-1 is a transcription factor involved in the cell cycle regulation of histone H2B gene transcription and in the transcription of other cellular housekeeping genes. Oct-1 is hyperphosphorylated as cells enter mitosis, and mitosis-specific phosphorylation is reversed as cells exit mitosis. A mitosis-specific phosphorylation site in the homeodomain of Oct-1 was phosphorylated in vitro by protein kinase A. Phosphorylation of this site correlated with inhibition of Oct-1 DNA binding activity in vivo and in vitro. The inhibition of Oct-1 DNA binding during mitosis suggests a mechanism by which the general inhibition of transcription during mitosis might occur.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Segil, N -- Roberts, S B -- Heintz, N -- GM 13752/GM/NIGMS NIH HHS/ -- GM 32544/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1814-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1684878" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Cell Cycle ; Cloning, Molecular ; DNA, Neoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Genes, Homeobox ; HeLa Cells ; Histones/genetics ; Host Cell Factor C1 ; Humans ; Mitosis ; Molecular Sequence Data ; Myocardium/enzymology ; Octamer Transcription Factor-1 ; Oligodeoxyribonucleotides ; Peptide Mapping ; Phosphopeptides/isolation & purification ; Phosphorylation ; Protein Kinases/metabolism ; Transcription Factors/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Identification of a zinc finger protein that inhibits IL-2 gene expression (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-20
    Description: Transient activation of the interleukin-2 (IL-2) gene after antigen recognition by T lymphocytes is crucial for subsequent T cell proliferation and differentiation. Several IL-2 gene regulatory elements and binding factors necessary for activation of the IL-2 gene have been defined. However, little is known about negative regulation of IL-2 expression, which is likely to be important in the rapid shut-off of IL-2 transcription. A nucleotide sequence element (NRE-A) that negatively regulates IL-2 expression has been identified within the IL-2 gene. T cell nuclear extracts contained an NRE-A binding activity. A complementary DNA was isolated that encodes a zinc finger-containing protein that suppressed IL-2 gene expression. The observation of negative regulation of the immunoglobulin heavy chain gene enhancer by an element similar to NRE-A suggests that related proteins may regulate multiple immune response genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, T M -- Moolten, D -- Burlein, J -- Romano, J -- Bhaerman, R -- Godillot, A -- Mellon, M -- Rauscher, F J 3rd -- Kant, J A -- AI23879/AI/NIAID NIH HHS/ -- CA23413/CA/NCI NIH HHS/ -- CA54428/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1791-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, School of Medicine, University of New Mexico, Albuquerque 87131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840704" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA Probes ; *Enhancer Elements, Genetic ; *Gene Expression Regulation ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Heavy Chains/*genetics ; Interleukin-2/*genetics ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Regulatory Sequences, Nucleic Acid ; Restriction Mapping ; T-Lymphocytes/*immunology ; *Transcription, Genetic ; Zinc Fingers/*genetics/physiology
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    Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-02
    Description: Epidermolysis bullosa simplex (EBS) is characterized by skin blistering due to basal keratinocyte fragility. In one family studied, inheritance of EBS is linked to the gene encoding keratin 14, and a thymine to cytosine mutation in exon 6 of keratin 14 has introduced a proline in the middle of an alpha-helical region. In a second family, inheritance of EBS is linked to loci that map near the keratin 5 gene. These data indicate that abnormalities of either of the components of the keratin intermediate filament heterodipolymer can impair the mechanical stability of these epithelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonifas, J M -- Rothman, A L -- Epstein, E H Jr -- R01-AR28069/AR/NIAMS NIH HHS/ -- R01-AR39953/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1202-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, San Francisco General Hospital, University of California 94110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720261" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Human, Pair 12 ; Chromosomes, Human, Pair 17 ; Epidermolysis Bullosa Simplex/*genetics ; Genes ; Genetic Linkage ; Humans ; Keratins/*genetics ; Molecular Sequence Data ; Oligonucleotides/chemistry ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length
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    Identification of p53 as a sequence-specific DNA-binding protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The tumor-suppressor gene p53 is altered by missense mutation in numerous human malignancies. However, the biochemical properties of p53 and the effect of mutation on these properties are unclear. A human DNA sequence was identified that binds specifically to wild-type human p53 protein in vitro. As few as 33 base pairs were sufficient to confer specific binding. Certain guanines within this 33-base pair region were critical, as methylation of these guanines or their substitution with thymine-abrogated binding. Human p53 proteins containing either of two missense mutations commonly found in human tumors were unable to bind significantly to this sequence. These data suggest that a function of p53 may be mediated by its ability to bind to specific DNA sequences in the human genome, and that this activity is altered by mutations that occur in human tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kern, S E -- Kinzler, K W -- Bruskin, A -- Jarosz, D -- Friedman, P -- Prives, C -- Vogelstein, B -- CA06973/CA/NCI NIH HHS/ -- CA33620/CA/NCI NIH HHS/ -- CA43460/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1708-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047879" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA Mutational Analysis ; DNA Replication ; DNA-Binding Proteins/*metabolism ; HeLa Cells ; Humans ; In Vitro Techniques ; Methylation ; Molecular Sequence Data ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Tumor Suppressor Protein p53/genetics/*metabolism
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    Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This bend results almost entirely from two 40 degrees kinks that occur between TG/CA base pairs at positions 5 and 6 on each side of the dyad axis of the complex. DNA sequence discrimination by CAP derives both from sequence-dependent distortion of the DNA helix and from direct hydrogen-bonding interactions between three protein side chains and the exposed edges of three base pairs in the major groove of the DNA. The structure of this transcription factor--DNA complex provides insights into possible mechanisms of transcription activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, S C -- Shields, G C -- Steitz, T A -- GM-22778/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1001-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653449" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Cyclic AMP Receptor Protein/*chemistry/metabolism ; DNA, Bacterial/*chemistry/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; X-Ray Diffraction/methods
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    An in vivo model of somatic cell gene therapy for human severe combined immunodeficiency (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-15
    Description: Deficiency of adenosine deaminase (ADA) results in severe combined immunodeficiency (SCID), a candidate genetic disorder for somatic cell gene therapy. Peripheral blood lymphocytes from patients affected by ADA- SCID were transduced with a retroviral vector for human ADA and injected into immunodeficient mice. Long-term survival of vector-transduced human cells was demonstrated in recipient animals. Expression of vector-derived ADA restored immune functions, as indicated by the presence in reconstituted animals of human immunoglobulin and antigen-specific T cells. Retroviral vector gene transfer, therefore, is necessary and sufficient for development of specific immune functions in vivo and has therapeutic potential to correct this lethal immunodeficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferrari, G -- Rossini, S -- Giavazzi, R -- Maggioni, D -- Nobili, N -- Soldati, M -- Ungers, G -- Mavilio, F -- Gilboa, E -- Bordignon, C -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Hematology, Istituto Scientifico H.S. Raffaele, Milano, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848369" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/*deficiency/genetics ; Animals ; Base Sequence ; Genetic Therapy ; Genetic Vectors ; Humans ; Immunologic Deficiency Syndromes/*genetics/therapy ; Kanamycin Kinase ; Lymphocyte Transfusion ; Lymphocytes/physiology ; Mice ; Mice, Mutant Strains ; Oligonucleotides/chemistry ; Phosphotransferases/genetics ; Polymerase Chain Reaction ; Retroviridae/genetics
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    Signal transduction by interferon-alpha through arachidonic acid metabolism (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-11
    Description: Molecular mechanisms that mediate signal transduction by growth inhibitory cytokines are poorly understood. Type I (alpha and beta) interferons (IFNs) are potent growth inhibitory cytokines whose biological activities depend on induced changes in gene expression. IFN-alpha induced the transient activation of phospholipase A2 in 3T3 fibroblasts and rapid hydrolysis of [3H]arachidonic acid (AA) from prelabeled phospholipid pools. The phospholipase inhibitor, bromophenacyl bromide (BPB), specifically blocked IFN-induced binding of nuclear factors to a conserved, IFN-regulated enhancer element, the interferon-stimulated response element (ISRE). BPB also caused a dose-dependent inhibition of IFN-alpha-induced ISRE-dependent transcription in transient transfection assays. Specific inhibition of AA oxygenation by eicosatetraynoic acid prevented IFN-alpha induction of factor binding to the ISRE. Treatment of intact cells with inhibitors of fatty acid cyclooxygenase or lipoxygenase enzymes resulted in amplification of IFN-alpha-induced ISRE binding and gene expression. Thus, IFN-alpha receptor-coupled AA hydrolysis may function in activation of latent transcription factors by IFN-alpha and provides a system for studying the role of AA metabolism in transduction of growth inhibitory signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hannigan, G E -- Williams, B R -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):204-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1898993" target="_blank"〉PubMed〈/a〉
    Keywords: 5,8,11,14-Eicosatetraynoic Acid/pharmacology ; Acetophenones/pharmacology ; Animals ; Arachidonic Acid ; Arachidonic Acids/*metabolism ; Base Sequence ; Cell Line ; Cyclooxygenase Inhibitors ; Enhancer Elements, Genetic ; Enzyme Activation ; Indomethacin/pharmacology ; Interferon Type I/*physiology ; Lipoxygenase Inhibitors ; Lysophosphatidylcholines/metabolism ; Masoprocol/pharmacology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Phospholipases A/antagonists & inhibitors/*metabolism ; Phospholipases A2 ; Platelet-Derived Growth Factor/pharmacology ; Second Messenger Systems ; *Signal Transduction ; Transcription Factors/metabolism ; Transcription, Genetic ; Transfection
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    Reverse transcriptase encoded by a human transposable element (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-30
    Description: L1 elements are highly repeated mammalian DNA sequences whose structure suggests dispersal by retrotransposition. A consensus L1 element encodes a protein with sequence similarity to known reverse transcriptases. The second open reading frame from the human L1 element L1.2A was expressed as a fusion protein targeted to Ty1 virus-like particles in Saccharomyces cerevisiae and shown to have reverse transcriptase activity. This activity was eliminated by a missense mutation in the highly conserved amino acid motif Y/F-X-D-D. Thus, L1 represents a potential source of the reverse transcriptase activity necessary for dispersion of the many classes of mammalian retroelements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathias, S L -- Scott, A F -- Kazazian, H H Jr -- Boeke, J D -- Gabriel, A -- AI00803/AI/NIAID NIH HHS/ -- CA16519/CA/NCI NIH HHS/ -- GM28931/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1722352" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; *DNA Transposable Elements ; Epitopes/analysis ; Humans ; Immunoblotting ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Open Reading Frames ; Plasmids ; Polyribonucleotides ; RNA-Directed DNA Polymerase/*genetics/isolation & purification/metabolism ; Recombinant Fusion Proteins/isolation & purification/metabolism ; Saccharomyces cerevisiae/genetics ; Templates, Genetic
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    Identification of a competitive HGF antagonist encoded by an alternative transcript (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: We identified a naturally occurring hepatocyte growth factor (HGF) variant, whose predicted sequence extends only through the second kringle domain of this plasminogen-related molecule. This smaller molecule, derived from an alternative HGF transcript, lacked mitogenic activity but specifically inhibited HGF-induced mitogenesis. Cross-linking studies demonstrated that the truncated molecule competes with HGF for binding to the HGF receptor, which has been identified as the c-met protooncogene product. Thus, the same gene encodes both a growth factor and its direct antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A M -- Rubin, J S -- Bottaro, D P -- Hirschfield, D W -- Chedid, M -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1382-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720571" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cell Line ; Culture Media ; DNA/genetics ; DNA Replication/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Hepatocyte Growth Factor ; Humans ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Plasmids ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger ; Thymidine/metabolism ; *Transcription, Genetic ; Transfection
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    Recognition of DNA by Cys2,His2 zinc fingers (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klevit, R E -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1367, 1393.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1896847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/*metabolism ; Molecular Sequence Data ; Zinc Fingers/*genetics/physiology
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    Inhibition of entry of HIV-1 in neural cell lines by antibodies against galactosyl ceramide (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-19
    Description: Although the CD4 molecule is the principal cellular receptor for the human immunodeficiency virus (HIV), several CD4-negative cell lines are susceptible to infection with one or more HIV strains. These findings indicate that there are alternate modes of viral entry, perhaps involving one or more receptor molecules. Antibodies against galactosyl ceramide (galactocerebroside, or GalC) inhibited viral internalization and infection in two CD4-negative cell lines derived from the nervous system: U373-MG and SK-N-MC. Furthermore, recombinant HIV surface glycoprotein gp120 bound to GalC but not to other glycolipids. These results suggest a role for GalC or a highly related molecule in HIV entry into neural cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harouse, J M -- Bhat, S -- Spitalnik, S L -- Laughlin, M -- Stefano, K -- Silberberg, D H -- Gonzalez-Scarano, F -- CA-45690/CA/NCI NIH HHS/ -- NS-11037/NS/NINDS NIH HHS/ -- NS-27405/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):320-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Pennsylvania Medical Center, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857969" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibodies ; Antigens, CD4/physiology ; Base Sequence ; Cell Line ; Galactosylceramides/*immunology ; Gene Products, gag/genetics ; Glioma ; HIV Envelope Protein gp120/immunology ; HIV-1/genetics/immunology/*physiology ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein Binding ; Recombinant Proteins/immunology
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    Functional importance of sequence in the stem-loop of a transcription terminator (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-22
    Description: Intrinsic transcription terminators of prokaryotes are distinguished by a common RNA motif: a stem-loop structure high in guanine and cytosine content, followed by multiple uridine residues. Models explaining intrinsic terminators postulate that the stem-loop sequence is necessary only to form structure. In the tR2 terminator of coliphage lambda, single-nucleotide changes reducing potential RNA stem stability eliminated tR2 activity, and a compensatory change that restored the stem structure restored terminator activity. However, multiple changes in the stem sequence that should have either maintained or increased stability reduced terminator activity. These results suggest that the ability of the stem-loop structure to signal transcription termination depends on sequence specificity and secondary structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, S W -- Lynch, E C -- Leason, K R -- Court, D L -- Shapiro, B A -- Friedman, D I -- AI1459-10/AI/NIAID NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1205-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1835546" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/*genetics ; Base Sequence ; DNA Mutational Analysis ; Gene Expression Regulation, Viral ; Genes, Viral ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Messenger/genetics ; RNA, Viral/genetics ; *Regulatory Sequences, Nucleic Acid ; Restriction Mapping ; *Terminator Regions, Genetic ; *Transcription, Genetic ; Viral Structural Proteins/genetics
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    p53 mutations in human cancers (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-05
    Description: Mutations in the evolutionarily conserved codons of the p53 tumor suppressor gene are common in diverse types of human cancer. The p53 mutational spectrum differs among cancers of the colon, lung, esophagus, breast, liver, brain, reticuloendothelial tissues, and hemopoietic tissues. Analysis of these mutations can provide clues to the etiology of these diverse tumors and to the function of specific regions of p53. Transitions predominate in colon, brain, and lymphoid malignancies, whereas G:C to T:A transversions are the most frequent substitutions observed in cancers of the lung and liver. Mutations at A:T base pairs are seen more frequently in esophageal carcinomas than in other solid tumors. Most transitions in colorectal carcinomas, brain tumors, leukemias, and lymphomas are at CpG dinucleotide mutational hot spots. G to T transversions in lung, breast, and esophageal carcinomas are dispersed among numerous codons. In liver tumors in persons from geographic areas in which both aflatoxin B1 and hepatitis B virus are cancer risk factors, most mutations are at one nucleotide pair of codon 249. These differences may reflect the etiological contributions of both exogenous and endogenous factors to human carcinogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hollstein, M -- Sidransky, D -- Vogelstein, B -- Harris, C C -- CA 09071/CA/NCI NIH HHS/ -- CA 43460/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):49-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1905840" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chickens ; DNA Mutational Analysis ; *Genes, p53 ; Haplorhini ; Humans ; Mice ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Rats ; Sequence Homology, Nucleic Acid ; Trout ; Xenopus
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    Sequence-selective recognition of DNA by strand displacement with a thymine-substituted polyamide (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-06
    Description: A polyamide nucleic acid (PNA) was designed by detaching the deoxyribose phosphate backbone of DNA in a computer model and replacing it with an achiral polyamide backbone. On the basis of this model, oligomers consisting of thymine-linked aminoethylglycyl units were prepared. These oligomers recognize their complementary target in double-stranded DNA by strand displacement. The displacement is made possible by the extraordinarily high stability of the PNA-DNA hybrids. The results show that the backbone of DNA can be replaced by a polyamide, with the resulting oligomer retaining base-specific hybridization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nielsen, P E -- Egholm, M -- Berg, R H -- Buchardt, O -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1497-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry B, Panum Institute, Copenhagen, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962210" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Molecular Sequence Data ; Molecular Structure ; Nylons/*chemistry ; Oligonucleotides/*chemistry ; Photochemistry ; Thermodynamics
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    Control of doublesex alternative splicing by transformer and transformer-2 in Drosophila (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: Sex-specific alternative processing of doublesex (dsx) precursor messenger RNA (pre-mRNA) regulates somatic sexual differentiation in Drosophila melanogaster. Cotransfection analyses in which the dsx gene and the female-specific transformer (tra) and transformer-2 (tra-2) complementary DNAs were expressed in Drosophila Kc cells revealed that female-specific splicing of the dsx transcript was positively regulated by the products of the tra and tra-2 genes. Furthermore, analyses of mutant constructs of dsx showed that a portion of the female-specific exon sequence was required for regulation of dsx pre-messenger RNA splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshijima, K -- Inoue, K -- Higuchi, I -- Sakamoto, H -- Shimura, Y -- New York, N.Y. -- Science. 1991 May 10;252(5007):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Faculty of Science, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902987" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; Drosophila melanogaster/*genetics ; Gene Expression Regulation ; Genes/physiology ; Genes, Regulator/physiology ; Molecular Sequence Data ; *RNA Splicing ; RNA, Messenger/biosynthesis ; Repetitive Sequences, Nucleic Acid ; Sex Differentiation/*physiology ; Transfection
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  • 81
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    Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-09
    Description: Previous studies suggested that one or more genes on chromosome 5q21 are responsible for the inheritance of familial adenomatous polyposis (FAP) and Gardner's syndrome (GS), and contribute to tumor development in patients with noninherited forms of colorectal cancer. Two genes on 5q21 that are tightly linked to FAP (MCC and APC) were found to be somatically altered in tumors from sporadic colorectal cancer patients. One of the genes (APC) was also found to be altered by point mutation in the germ line of FAP and GS patients. These data suggest that more than one gene on chromosome 5q21 may contribute to colorectal neoplasia, and that mutations of the APC gene can cause both FAP and GS. The identification of these genes should aid in understanding the pathogenesis of colorectal neoplasia and in the diagnosis and counseling of patients with inherited predispositions to colorectal cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishisho, I -- Nakamura, Y -- Miyoshi, Y -- Miki, Y -- Ando, H -- Horii, A -- Koyama, K -- Utsunomiya, J -- Baba, S -- Hedge, P -- CA06973/CA/NCI NIH HHS/ -- CA35494/CA/NCI NIH HHS/ -- CA44688/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 9;253(5020):665-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Cancer Institute, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1651563" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/*genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 5 ; Codon/genetics ; Colonic Neoplasms/*genetics ; DNA, Neoplasm/genetics/isolation & purification ; Genetic Linkage ; Genetic Variation ; Humans ; Molecular Sequence Data ; *Mutation ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Rectal Neoplasms/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    LAV revisited: origins of the early HIV-1 isolates from Institut Pasteur (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-17
    Description: Two of the first human immunodeficiency virus type-1 (HIV-1) strains isolated were authenticated by reanalyzing original cultured samples stored at the Collection Nationale de Culture des Microorganismes as well as uncultured primary material. Cloned polymerase chain reaction products were used to analyze coding sequences of the V3 loop in the gp120 glycoprotein. The original isolate HIV-1 Bru, formerly called LAV, was derived from patient BRU. HIV-1 Lai was derived from patient LAI and contaminated a HIV-1 Bru culture between 20 July and 3 August 1983. The culture became, in effect, HIV-1 Lai, identifiable by a unique motif in the V3 loop. Because of this contamination two, rather than one, HIV-1 isolates were sent to the Laboratory of Tumor Cell Biology at the National Cancer Institute on 23 September 1983. Original HIV-1 Bru was indeed present in the sample marked JBB/LAV. However the M2T-/B sample harbored HIV-1 Lai, a strain capable of growing on established cell lines. The striking similarity between HIV-1 Lai (formerly LAV-Bru) and HTLV-3B sequences remains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wain-Hobson, S -- Vartanian, J P -- Henry, M -- Chenciner, N -- Cheynier, R -- Delassus, S -- Martins, L P -- Sala, M -- Nugeyre, M T -- Guetard, D -- New York, N.Y. -- Science. 1991 May 17;252(5008):961-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Retrovirologie Moleculaire, Institut Pasteur, Paris.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2035026" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; Acquired Immunodeficiency Syndrome/*microbiology/pathology ; Amino Acid Sequence ; Base Sequence ; Biopsy ; Cell Line ; Cloning, Molecular ; DNA, Viral/genetics/isolation & purification ; France ; HIV Envelope Protein gp120/*genetics ; HIV-1/classification/genetics/growth & development/*isolation & purification ; Humans ; Lymph Nodes/microbiology/pathology ; Male ; Molecular Sequence Data ; National Institutes of Health (U.S.) ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Sequence Homology, Nucleic Acid ; United States ; Virology/methods
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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    Possible horizontal transfer of Drosophila genes by the mite Proctolaelaps regalis (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-06
    Description: There is strong inferential evidence for recent horizontal gene transfer of the P (mobile) element to Drosophila melanogaster from a species of the Drosophila willistoni group. One potential vector of this transfer is a semiparasitic mite, Proctolaelaps regalis DeLeon, whose morphology, behavior, and co-occurrence with Drosophila are consistent with the properties necessary for such a vector. Southern blot hybridization, polymerase chain reaction (PCR) amplification, and DNA sequencing showed that samples of P. regalis associated with a P strain of D. melanogaster carried P element sequences. Similarly, Drosophila ribosomal DNA sequences were identified in P. regalis samples that had been associated with Drosophila cultures. These results have potentially important evolutionary implications, not only for understanding the mechanisms by which genes may be transferred between reproductively isolated species, but also for improved detection of some host-parasite and predator-prey relationships.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Houck, M A -- Clark, J B -- Peterson, K R -- Kidwell, M G -- 36715/PHS HHS/ -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1125-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of Arizona, Tucson 85721.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Blotting, Southern ; DNA/genetics/isolation & purification ; *DNA Transposable Elements ; DNA, Ribosomal/genetics ; Drosophila/*genetics ; Drosophila melanogaster/*genetics/parasitology/ultrastructure ; Microscopy, Electron, Scanning ; Mites/*genetics/physiology/ultrastructure ; Molecular Sequence Data ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Pupa ; *Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 84
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    Activation of early gene expression in T lymphocytes by Oct-1 and an inducible protein, OAP40 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: After antigenic stimulation of T lymphocytes, genes essential for proliferation and immune function, such as the interleukin-2 (IL-2) gene, are transcriptionally activated. In both transient transfections and T lymphocyte-specific in vitro transcription, the homeodomain-containing protein Oct-1 participated in the inducible regulation of transcription of the IL-2 gene. Oct-1 functioned in this context with a 40-kilodalton protein called Oct-1-associated protein (OAP40). In addition to interacting specifically with DNA, OAP40 reduced the rate of dissociation of Oct-1 from its cognate DNA-binding site, suggesting that a direct interaction exists between Oct-1 and OAP40.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullman, K S -- Flanagan, W M -- Edwards, C A -- Crabtree, G R -- AI07290/AI/NIAID NIH HHS/ -- CA39612/CA/NCI NIH HHS/ -- HL33942/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):558-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1683003" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Base Sequence ; DNA-Binding Proteins/biosynthesis/*genetics/*physiology ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Genes, Homeobox ; Host Cell Factor C1 ; Interleukin-2/*genetics ; Mice ; Mice, Inbred BALB C/immunology ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Oligodeoxyribonucleotides ; Peptides/chemical synthesis/immunology ; Rats ; T-Lymphocytes/immunology/*physiology ; Transcription Factors/*genetics/physiology ; *Transcription, Genetic ; Transfection
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  • 85
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    Antigenic diversity thresholds and the development of AIDS (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-15
    Description: Longitudinal studies of patients infected with HIV-1 reveal a long and variable incubation period between infection and the development of AIDS. Data from a small number of infected patients show temporal changes in the number of genetically distinct strains of the virus throughout the incubation period, with a slow but steady rise in diversity during the progression to disease. A mathematical model of the dynamic interaction between viral diversity and the human immune system suggests the existence of an antigen diversity threshold, below which the immune system is able to regulate viral population growth but above which the virus population induces the collapse of the CD4+ lymphocyte population. The model suggests that antigenic diversity is the cause, not a consequence, of immunodeficiency disease. The model is compared with available data, and is used to assess how the timing of the application of chemotherapy or immunotherapy influences the rate of progress to disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, M A -- Anderson, R M -- McLean, A R -- Wolfs, T F -- Goudsmit, J -- May, R M -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):963-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1683006" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/prevention & control/therapy ; Base Sequence ; CD4-Positive T-Lymphocytes ; Computer Simulation ; DNA, Viral/genetics ; HIV Antigens/genetics ; HIV Core Protein p24/metabolism ; HIV-1/genetics/*immunology ; Humans ; Immunotherapy ; Leukocyte Count ; Molecular Sequence Data ; Mutation ; Oligonucleotides/chemistry ; Time Factors ; Vaccination
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 86
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    Distinct protein targets for signals acting at the c-fos serum response element (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-11
    Description: The c-fos serum response element (SRE) is a primary nuclear target for intracellular signal transduction pathways triggered by growth factors. It is the target for both protein kinase C (PKC)-dependent and -independent signals. Function of the SRE requires binding of a cellular protein, termed serum response factor (SRF). A second protein, p62TCF, recognizes the SRE-SRF complex to form a ternary complex. A mutated SRE that bound SRF but failed to form the ternary complex selectively lost response to PKC activators, but retained response to PKC-independent signals. Thus, two different signaling pathways act through discrete nuclear targets at the SRE. At least one of these pathways functions by recruitment of a pathway-specific accessory factor (p62TCF). These results offer a molecular mechanism to account for the biological specificity of signals that appear to act through common DNA sequence elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graham, R -- Gilman, M -- AI27270/AI/NIAID NIH HHS/ -- CA45642/CA/NCI NIH HHS/ -- CA46370/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):189-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1898992" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Blood ; Cell Line ; DNA/metabolism ; *Enhancer Elements, Genetic ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutagenesis ; Nuclear Proteins/*metabolism ; Promoter Regions, Genetic/genetics ; Protein Kinase C/metabolism ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-fos ; Second Messenger Systems ; Serum Response Factor ; *Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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  • 87
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    The receptor for ciliary neurotrophic factor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-05
    Description: Although neurotrophic factors were originally isolated on the basis of their ability to support the survival of neurons, these molecules are now thought to influence many aspects of the development and maintenance of the nervous system. Identifying the receptors for these neurotrophic factors should aid in identifying the cells on which these factors act and in understanding their precise mechanisms of action. A "tagged-ligand panning" procedure was used to clone a receptor for ciliary neurotrophic factor (CNTF). This receptor is expressed exclusively within the nervous system and skeletal muscle. The CNTF receptor has a structure unrelated to the receptors utilized by the nerve growth factor family of neurotrophic molecules, but instead is most homologous to the receptor for a cytokine, interleukin-6. This similarity suggestes that the CNTF receptor, like the interleukin-6 receptor, requires a second, signal-transducing component. In contrast to all known receptors, the CNTF receptor is anchored to cell membranes by a glycosyl-phosphatidylinositol linkage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Valenzuela, D M -- Wong, V V -- Furth, M E -- Squinto, S P -- Yancopoulos, G D -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):59-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648265" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; Electrophoresis, Agar Gel ; Gene Expression ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Muscles/metabolism ; Nervous System/metabolism ; Neuroblastoma/metabolism ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/blood/*genetics ; Sequence Homology, Nucleic Acid ; Transfection
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  • 88
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    Dependence of kidney morphogenesis on the expression of nerve growth factor receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: Nerve growth factor receptor (NGFR) serves as the binding site for the neurotrophic growth factors. Although NGFR has been found in several embryonic tissues outside the nervous system, the function of NGFR in embryogenesis of non-neuronal organs remains unknown. NGFR is transiently synthesized by embryonic rat kidney and disappears from nephrons upon their terminal differentiation. Anti-sense oligonucleotide inhibition of NGFR expression inhibits kidney morphogenesis. Therefore, NGFR is required not only for development of the nervous system, but also for differentiation of the kidney tubules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sariola, H -- Saarma, M -- Sainio, K -- Arumae, U -- Palgi, J -- Vaahtokari, A -- Thesleff, I -- Karavanov, A -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):571-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Paediatric Pathology, Childrens' Hospital, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658930" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Embryo, Mammalian ; Gene Expression ; Kidney/cytology/*embryology ; Molecular Sequence Data ; Nerve Growth Factors/*physiology ; Oligonucleotides, Antisense ; PC12 Cells ; RNA, Messenger/analysis/genetics ; Rats ; Receptors, Cell Surface/*genetics/physiology ; Receptors, Nerve Growth Factor
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  • 89
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    A distinct potassium channel polypeptide encoded by the Drosophila eag locus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-14
    Description: Many of the signaling properties of neurons and other electrically excitable cells are determined by a diverse family of potassium channels. A number of genes that encode potassium channel polypeptides have been cloned from various organisms on the basis of their sequence similarity to the Drosophila Shaker (Sh) locus. As an alternative strategy, a molecular analysis of other Drosophila genes that were defined by mutations that perturb potassium channel function was undertaken. Sequence analysis of complementary DNA from the ether a go-go (eag) locus revealed that it encodes a structural component of potassium channels that is related to but is distinct from all identified potassium channel polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warmke, J -- Drysdale, R -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840699" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; DNA/genetics ; Drosophila/*genetics ; Molecular Sequence Data ; Potassium Channels/*genetics ; Protein Conformation ; Sequence Homology, Nucleic Acid
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  • 90
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    An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-04-05
    Description: Derivatives of erythromycin with modifications at their C-6 position are generally sought for their increased stability at acid pH, which in turn may confer improved pharmacological properties. A recombinant mutant of the erythromycin-producing bacterium, Saccharopolyspora erythraea, produced an erythromycin derivative, 6-deoxyerythromycin A, that could not be obtained readily by chemical synthesis. This product resulted from targeted disruption of the gene, designated eryF (systematic nomenclature, CYP107), that apparently codes for the cytochrome P450, 6-deoxyerythronolide B (DEB) hydroxylase, which converts DEB to erythronolide B (EB). Enzymes normally acting on EB can process the alternative substrate DEB to form the biologically active erythromycin derivative lacking the C-6 hydroxyl group.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, J M -- Leung, J O -- Swanson, S J -- Idler, K B -- McAlpine, J B -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BioProcess Development, Department 451/R5, Abbott Laboratories, North Chicago, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011746" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteria/genetics ; Bacterial Proteins ; Base Sequence ; Cytochrome P-450 Enzyme System/*genetics ; DNA Mutational Analysis ; DNA, Bacterial/genetics ; Erythromycin/analogs & derivatives/*biosynthesis ; *Genes, Bacterial ; Mixed Function Oxygenases/*genetics ; Molecular Sequence Data ; Plasmids ; Restriction Mapping
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  • 91
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    Selective depletion in HIV infection of T cells that bear specific T cell receptor V beta sequences (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: The mechanism of T cell depletion during infection with the human immunodeficiency virus (HIV) is unclear. Examination of the repertoire of T cell receptor V (variable) regions in persons infected with HIV revealed the absence of a common set of V beta regions, whereas V alpha usage was normal. The lack of these V beta segments did not appear to correlate with opportunistic infections. The selective elimination of T cells that express a defined set of V beta sequences may indicate the presence of an HIV-encoded superantigen, similar to those encoded by the long terminal repeat of the mouse mammary tumor virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imberti, L -- Sottini, A -- Bettinardi, A -- Puoti, M -- Primi, D -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):860-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Consorzio per le Biotecnologie-Consiglio Nazionale delle Ricerche-Institute of Chemistry, School of Medicine, University of Brescia, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948066" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/genetics/*immunology ; Base Sequence ; Blotting, Southern ; DNA/genetics/isolation & purification ; HIV/immunology ; HIV Infections/genetics/*immunology ; Humans ; *Lymphocyte Depletion ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Receptors, Antigen, T-Cell/*genetics ; Reference Values ; T-Lymphocytes/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Retronphage phi R73: an E. coli phage that contains a retroelement and integrates into a tRNA gene (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-17
    Description: Some strains of Escherichia coli contain retroelements (retrons) that encode genes for reverse transcriptase and branched, multicopy, single-stranded DNA (msDNA) linked to RNA. However, the origin of retrons is unknown. A P4-like cryptic prophage was found that contains a retroelement (retron Ec73) for msDNA-Ec73 in an E. coli clinical strain. The entire genome of this prophage, named phi R73, is 12.7 kilobase pairs and is flanked by 29-base pair direct repeats derived from the 3' end of the selenocystyl transfer RNA gene (selC). P2 bacteriophage caused excision of the phi R73 prophage and acted as a helper to package phi R73 DNA into an infectious virion. The newly formed phi R73 closely resembled P4 as a virion and in its lytic growth. Retronphage phi R73 lysogenized a new host strain, reintegrating its genome into the selC gene of the host chromosome and enabling the newly formed lysogens to produce msDNA-Ec73. Hence, retron Ec73 can be transferred intercellularly as part of the genome of a helper-dependent retronphage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Sunshine, M G -- Six, E W -- Inouye, M -- AI04043/AI/NIAID NIH HHS/ -- GM44012/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):969-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey at Rutgers, Piscataway 08854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709758" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Coliphages/*genetics/ultrastructure ; DNA, Bacterial/genetics ; DNA, Viral/genetics ; Escherichia coli/*genetics ; *Genes, Bacterial ; *Genes, Viral ; Microscopy, Electron ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Open Reading Frames ; RNA, Transfer/*genetics ; RNA-Directed DNA Polymerase/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Messenger RNA splicing in yeast: clues to why the spliceosome is a ribonucleoprotein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The removal of introns from eukaryotic messenger RNA precursors shares mechanistic characteristics with the self-splicing of certain introns, prompting speculation that the catalytic reactions of nuclear pre-messenger RNA splicing are fundamentally RNA-based. The participation of five small nuclear RNAs (snRNAs) in splicing is now well documented. Genetic analysis in yeast has revealed the requirement, in addition, for several dozen proteins. Some of these are tightly bound to snRNAs to form small nuclear ribonucleoproteins (snRNPs); such proteins may promote interactions between snRNAs or between an snRNA and the intron. Other, non-snRNP proteins appear to associate transiently with the spliceosome. Some of these factors, which include RNA-dependent adenosine triphosphatases, may promote the accurate recognition of introns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):157-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853200" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/physiology ; Base Sequence ; Fungal Proteins/genetics ; Molecular Sequence Data ; *RNA Splicing ; RNA, Fungal/*genetics ; RNA, Messenger/*genetics ; RNA, Small Nuclear/genetics ; Ribonucleoproteins/*physiology ; Saccharomyces cerevisiae/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Organizer-specific homeobox genes in Xenopus laevis embryos (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The dorsal blastopore lip of the early Xenopus laevis gastrula can organize a complete secondary body axis when transplanted to another embryo. A search for potential gene regulatory components specifically expressed in the organizer was undertaken that resulted in the identification of four types of complementary DNAs from homeobox-containing genes that fulfill this criterion. The most abundant of these encodes a DNA-binding specificity similar to that of the Drosophila melanogaster anterior morphogen bicoid. The other three are also homologous to developmentally significant Drosophila genes. These four genes may participate in the regulation of the developmental potential of the organizer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blumberg, B -- Wright, C V -- De Robertis, E M -- Cho, K W -- HD-07273/HD/NICHD NIH HHS/ -- HD-21502/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):194-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677215" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; DNA/genetics ; DNA-Binding Proteins/*physiology ; Embryonic Induction ; Gene Expression ; Gene Library ; *Genes, Homeobox ; Molecular Sequence Data ; Morphogenesis ; Oligonucleotides/chemistry ; RNA, Messenger/genetics ; Xenopus laevis/*embryology/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Deposits of amyloid beta protein in the central nervous system of transgenic mice (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-19
    Description: Alzheimer's disease is characterized by widespread deposition of amyloid in the central nervous system. The 4-kilodalton amyloid beta protein is derived from a larger amyloid precursor protein and forms amyloid deposits in the brain by an unknown pathological mechanism. Except for aged nonhuman primates, there is no animal model for Alzheimer's disease. Transgenic mice expressing amyloid beta protein in the brain could provide such a model. To investigate this possibility, the 4-kilodalton human amyloid beta protein was expressed under the control of the promoter of the human amyloid precursor protein in two lines of transgenic mice. Amyloid beta protein accumulated in the dendrites of some but not all hippocampal neurons in 1-year-old transgenic mice. Aggregates of the amyloid beta protein formed amyloid-like fibrils that are similar in appearance to those in the brains of patients with Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirak, D O -- Bayney, R -- Ramabhadran, T V -- Fracasso, R P -- Hart, J T -- Hauer, P E -- Hsiau, P -- Pekar, S K -- Scangos, G A -- Trapp, B D -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):323-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Therapeutics Inc., Miles Research Center, West Haven, CT 06516.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857970" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/pathology ; Amyloid beta-Peptides/analysis/*genetics ; Animals ; Base Sequence ; Brain/*metabolism/pathology ; DNA/genetics ; Hippocampus/ultrastructure ; Humans ; Mice ; Mice, Transgenic ; Microscopy, Electron ; Molecular Sequence Data ; Neurofibrils/ultrastructure ; Oligonucleotide Probes ; Restriction Mapping
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Cloning and expression of a cocaine-sensitive dopamine transporter complementary DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: A rat dopamine (DA) transporter complementary DNA has been isolated with combined complementary DNA homology and expression approaches. The DA transporter is a 619-amino acid protein with 12 hydrophobic putative membrane-spanning domains and homology to the norepinephrine and gamma-aminobutyric acid transporters. The expressed complementary DNA confers transport of [3H]DA in Xenopus oocytes and in COS cells. Binding of the cocaine analog [3H]CFT ([3H]2 beta-carbomethoxy-3 beta-(4-fluorophenyl)tropane) to transfected COS cell membranes yields a pharmacological profile similar to that in striatal membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimada, S -- Kitayama, S -- Lin, C L -- Patel, A -- Nanthakumar, E -- Gregor, P -- Kuhar, M -- Uhl, G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):576-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology, National Institute on Drug Abuse, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948034" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cloning, Molecular ; Cocaine/analogs & derivatives/metabolism/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Female ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Models, Structural ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Oocytes/physiology ; Plasmids ; Polymerase Chain Reaction ; Protein Conformation ; RNA, Messenger/genetics ; Rats ; Transcription, Genetic ; Transfection ; Xenopus
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    In vivo footprinting of MHC class II genes: bare promoters in the bare lymphocyte syndrome (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: Major histocompatibility complex (MHC) class II genes are coordinately regulated and show tissue-specific expression. With the use of in vivo footprinting, common promoter sites in these genes were found to be occupied only in cells that expressed the genes, in spite of the presence of the promoter binding proteins. In vivo analysis of mutant cell lines that exhibited coordinate loss of class II MHC expression, including several from individuals with bare lymphocyte syndrome, revealed two in vivo phenotypes. One suggests a defect in gene activation, whereas the other suggests a defect in promoter accessibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kara, C J -- Glimcher, L H -- AI21163/AI/NIAID NIH HHS/ -- GM36864/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902592" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Cell Line ; DNA/genetics ; *Gene Expression ; Genes, MHC Class II/*genetics ; Humans ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; *Promoter Regions, Genetic ; Regulatory Sequences, Nucleic Acid ; Syndrome
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Cloning and expression of the cDNA for human gamma-glutamyl carboxylase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: The cDNA for human gamma-glutamyl carboxylase, which accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins, was cloned. The enzyme is a 758-residue integral membrane protein and appears to have three transmembrane domains near its amino terminus. The hydrophilic COOH-terminal half of the carboxylase has 19.3 percent identity with soybean seed lipoxygenase. Expression of the cloned cDNA resulted in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, S M -- Cheung, W F -- Frazier, D -- Stafford, D W -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1634-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill 27599-3280.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Carbon-Carbon Ligases ; Cattle ; Cloning, Molecular ; DNA/genetics ; Humans ; Ligases/*genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; Recombinant Proteins ; Sequence Alignment
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Defining protective responses to pathogens: cytokine profiles in leprosy lesions (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-11
    Description: The immunological mechanisms required to engender resistance have been defined in few infectious diseases of man, and the role of specific cytokines is unclear. Leprosy presents clinically as a spectrum in which resistance correlates with cell-mediated immunity to the pathogen. To assess in situ cytokine patterns, messenger RNA extracted from leprosy skin biopsy specimens was amplified by the polymerase chain reaction with 14 cytokine-specific primers. In lesions of the resistant form of the disease, messenger RNAs coding for interleukin-2 and interferon-gamma were most evident. In contrast, messenger RNAs for interleukin-4, interleukin-5, and interleukin-10 predominated in the multibacillary form. Thus, resistance and susceptibility were correlated with distinct patterns of cytokine production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamura, M -- Uyemura, K -- Deans, R J -- Weinberg, K -- Rea, T H -- Bloom, B R -- Modlin, R L -- AI 07118/AI/NIAID NIH HHS/ -- AI 22553/AI/NIAID NIH HHS/ -- AR 40312/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):277-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Dermatology, UCLA School of Medicine 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925582" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cytokines/genetics/*physiology ; Humans ; Immunity, Innate ; Interferon-gamma/physiology ; Interleukin-10/physiology ; Interleukin-2/physiology ; Interleukin-4/physiology ; Interleukin-5/physiology ; Leprosy/*immunology ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Skin/immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Molecular transfer of a species-specific behavior from Drosophila simulans to Drosophila melanogaster (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: Drosophila males modulate the interpulse intervals produced during their courtship songs. These song cycles, which are altered by mutations in the clock gene period, exhibit a species-specific variation that facilitates mating. We have used chimeric period gene constructs from Drosophila melanogaster and Drosophila simulans in germline transformation experiments to map the genetic control of their song rhythm difference to a small segment of the amino acid encoding information within this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wheeler, D A -- Kyriacou, C P -- Greenacre, M L -- Yu, Q -- Rutila, J E -- Rosbash, M -- Hall, J C -- GM-21473/GM/NIGMS NIH HHS/ -- GM-33205/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1082-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900131" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Circadian Rhythm ; Drosophila/*physiology ; Drosophila melanogaster/*physiology ; Genes ; Molecular Sequence Data ; Motor Activity/physiology ; Restriction Mapping ; Sexual Behavior, Animal/*physiology ; Species Specificity ; Transfection ; Vocalization, Animal/physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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